Solution NMR structure of the helicase associated domain BVU-0683(627-691) from Bacteroides vulgatus provides first structural coverage for protein domain family PF03457 and indicates domain binding to DNA

Jeffrey L. Mills; Thomas B. Acton; Rong Xiao; John K. Everett; Gaetano T. Montelione; Thomas Szyperski

doi:10.1007/s10969-012-9148-0

Solution NMR structure of the helicase associated domain BVU-0683(627-691) from Bacteroides vulgatus provides first structural coverage for protein domain family PF03457 and indicates domain binding to DNA

Jeffrey L. Mills, Thomas B. Acton, Rong Xiao, John K. Everett, Gaetano T. Montelione, Thomas Szyperski

Research output: Contribution to journal › Article › peer-review

Abstract

A high-quality NMR structure of the helicase associated (HA) domain comprising residues 627-691 of the 753-residue protein BVU-0683 from Bacteroides vulgatus exhibits an all α-helical fold. The structure presented here is the first representative for the large protein domain family PF03457 (currently 742 members) of HA domains. Comparison with structurally similar proteins supports the hypothesis that HA domains bind to DNA and that binding specificity varies greatly within the family of HA domains constituting PF03457.

Original language	English (US)
Pages (from-to)	19-24
Number of pages	6
Journal	Journal of Structural and Functional Genomics
Volume	14
Issue number	1
DOIs	https://doi.org/10.1007/s10969-012-9148-0
State	Published - Mar 2013

All Science Journal Classification (ASJC) codes

Structural Biology
Biochemistry
Genetics

Keywords

A6KY75-BACV8
BVU-0683
Helicase associated domain
PF03457
SANT domain
Structural genomics

Access to Document

10.1007/s10969-012-9148-0

Fingerprint

Dive into the research topics of 'Solution NMR structure of the helicase associated domain BVU-0683(627-691) from Bacteroides vulgatus provides first structural coverage for protein domain family PF03457 and indicates domain binding to DNA'. Together they form a unique fingerprint.

Cite this

Mills, J. L., Acton, T. B., Xiao, R., Everett, J. K., Montelione, G. T., & Szyperski, T. (2013). Solution NMR structure of the helicase associated domain BVU-0683(627-691) from Bacteroides vulgatus provides first structural coverage for protein domain family PF03457 and indicates domain binding to DNA. Journal of Structural and Functional Genomics, 14(1), 19-24. https://doi.org/10.1007/s10969-012-9148-0

@article{b37e2f6649a0483c988973b6aa2a606d,

title = "Solution NMR structure of the helicase associated domain BVU-0683(627-691) from Bacteroides vulgatus provides first structural coverage for protein domain family PF03457 and indicates domain binding to DNA",

abstract = "A high-quality NMR structure of the helicase associated (HA) domain comprising residues 627-691 of the 753-residue protein BVU-0683 from Bacteroides vulgatus exhibits an all α-helical fold. The structure presented here is the first representative for the large protein domain family PF03457 (currently 742 members) of HA domains. Comparison with structurally similar proteins supports the hypothesis that HA domains bind to DNA and that binding specificity varies greatly within the family of HA domains constituting PF03457.",

keywords = "A6KY75-BACV8, BVU-0683, Helicase associated domain, PF03457, SANT domain, Structural genomics",

author = "Mills, {Jeffrey L.} and Acton, {Thomas B.} and Rong Xiao and Everett, {John K.} and Montelione, {Gaetano T.} and Thomas Szyperski",

note = "Funding Information: Acknowledgments We thank R. Belote, C. Ciccosanti, K. Hamilton, and G.V.T. Swapna for helpful discussions and technical support. This work was supported by the National Institutes of Health, grant number: U54 GM094597 (T.S. and G.T.M.).",

year = "2013",

month = mar,

doi = "10.1007/s10969-012-9148-0",

language = "English (US)",

volume = "14",

pages = "19--24",

journal = "Journal of Structural and Functional Genomics",

issn = "1345-711X",

publisher = "Springer Netherlands",

number = "1",

}

Mills, JL, Acton, TB, Xiao, R, Everett, JK, Montelione, GT & Szyperski, T 2013, 'Solution NMR structure of the helicase associated domain BVU-0683(627-691) from Bacteroides vulgatus provides first structural coverage for protein domain family PF03457 and indicates domain binding to DNA', Journal of Structural and Functional Genomics, vol. 14, no. 1, pp. 19-24. https://doi.org/10.1007/s10969-012-9148-0

Solution NMR structure of the helicase associated domain BVU-0683(627-691) from Bacteroides vulgatus provides first structural coverage for protein domain family PF03457 and indicates domain binding to DNA. / Mills, Jeffrey L.; Acton, Thomas B.; Xiao, Rong et al.

In: Journal of Structural and Functional Genomics, Vol. 14, No. 1, 03.2013, p. 19-24.

Research output: Contribution to journal › Article › peer-review

TY - JOUR

T1 - Solution NMR structure of the helicase associated domain BVU-0683(627-691) from Bacteroides vulgatus provides first structural coverage for protein domain family PF03457 and indicates domain binding to DNA

AU - Mills, Jeffrey L.

AU - Acton, Thomas B.

AU - Xiao, Rong

AU - Everett, John K.

AU - Montelione, Gaetano T.

AU - Szyperski, Thomas

N1 - Funding Information: Acknowledgments We thank R. Belote, C. Ciccosanti, K. Hamilton, and G.V.T. Swapna for helpful discussions and technical support. This work was supported by the National Institutes of Health, grant number: U54 GM094597 (T.S. and G.T.M.).

PY - 2013/3

Y1 - 2013/3

N2 - A high-quality NMR structure of the helicase associated (HA) domain comprising residues 627-691 of the 753-residue protein BVU-0683 from Bacteroides vulgatus exhibits an all α-helical fold. The structure presented here is the first representative for the large protein domain family PF03457 (currently 742 members) of HA domains. Comparison with structurally similar proteins supports the hypothesis that HA domains bind to DNA and that binding specificity varies greatly within the family of HA domains constituting PF03457.

AB - A high-quality NMR structure of the helicase associated (HA) domain comprising residues 627-691 of the 753-residue protein BVU-0683 from Bacteroides vulgatus exhibits an all α-helical fold. The structure presented here is the first representative for the large protein domain family PF03457 (currently 742 members) of HA domains. Comparison with structurally similar proteins supports the hypothesis that HA domains bind to DNA and that binding specificity varies greatly within the family of HA domains constituting PF03457.

KW - A6KY75-BACV8

KW - BVU-0683

KW - Helicase associated domain

KW - PF03457

KW - SANT domain

KW - Structural genomics

UR - http://www.scopus.com/inward/record.url?scp=84876793330&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84876793330&partnerID=8YFLogxK

U2 - 10.1007/s10969-012-9148-0

DO - 10.1007/s10969-012-9148-0

M3 - Article

C2 - 23160728

AN - SCOPUS:84876793330

SN - 1345-711X

VL - 14

SP - 19

EP - 24

JO - Journal of Structural and Functional Genomics

JF - Journal of Structural and Functional Genomics

IS - 1

ER -

Mills JL, Acton TB, Xiao R, Everett JK, Montelione GT, Szyperski T. Solution NMR structure of the helicase associated domain BVU-0683(627-691) from Bacteroides vulgatus provides first structural coverage for protein domain family PF03457 and indicates domain binding to DNA. Journal of Structural and Functional Genomics. 2013 Mar;14(1):19-24. doi: 10.1007/s10969-012-9148-0

Solution NMR structure of the helicase associated domain BVU-0683(627-691) from Bacteroides vulgatus provides first structural coverage for protein domain family PF03457 and indicates domain binding to DNA

Abstract

All Science Journal Classification (ASJC) codes

Keywords

Access to Document

Other files and links

Fingerprint

Cite this