The structure of the first representative of Pfam family PF06475 reveals a new fold with possible involvement in glycolipid metabolism

被引:7
作者
Bakolitsa, Constantina [1 ]
Kumar, Abhinav [2 ]
McMullan, Daniel [3 ]
Krishna, S. Sri [1 ,4 ]
Miller, Mitchell D. [2 ]
Carlton, Dennis [5 ]
Najmanovich, Rafael [6 ]
Abdubek, Polat [3 ]
Astakhova, Tamara [4 ]
Chiu, Hsiu-Ju [2 ]
Clayton, Thomas [5 ]
Deller, Marc C. [5 ]
Duan, Lian [4 ]
Elias, Ylva [5 ]
Feuerhelm, Julie [3 ]
Grant, Joanna C. [3 ]
Grzechnik, Slawomir K. [4 ]
Han, Gye Won [5 ]
Jaroszewski, Lukasz [1 ,4 ]
Jin, Kevin K. [2 ]
Klock, Heath E. [3 ]
Knuth, Mark W. [3 ]
Kozbial, Piotr [1 ]
Marciano, David [5 ]
Morse, Andrew T. [4 ]
Nigoghossian, Edward [3 ]
Okach, Linda [3 ]
Oommachen, Silvya [2 ]
Paulsen, Jessica [3 ]
Reyes, Ron [2 ]
Rife, Christopher L. [2 ]
Trout, Christina V. [5 ]
van den Bedem, Henry [2 ]
Weekes, Dana [1 ]
White, Aprilfawn [3 ]
Xu, Qingping [2 ]
Hodgson, Keith O.
Wooley, John [4 ]
Elsliger, Marc-Andre [5 ]
Deacon, Ashley M. [2 ]
Godzik, Adam [1 ,4 ]
Lesley, Scott A. [3 ,5 ]
Wilson, Ian A. [5 ]
机构
[1] Burnham Inst Med Res, Program Bioinformat & Syst Biol, La Jolla, CA USA
[2] SLAC Natl Accelerator Lab, Stanford Synchrotron Radiat Lightsource, Menlo Pk, CA USA
[3] Novartis Res Fdn, Genom Inst, Prot Sci Dept, San Diego, CA USA
[4] Univ Calif San Diego, Ctr Res Biol Syst, La Jolla, CA 92093 USA
[5] Scripps Res Inst, Dept Mol Biol, La Jolla, CA 92037 USA
[6] Univ Sherbrooke, Dept Biochim, Quebec City, PQ, Canada
来源
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2010年 / 66卷
基金
美国国家卫生研究院;
关键词
PROTEIN-STRUCTURE; CELL-WALL; ANGSTROM RESOLUTION; HYDROPHOBIC CAVITY; CRYSTAL-STRUCTURE; BINDING; LOLA; LIPOPOLYSACCHARIDE; DEHYDROGENASE; BIOSYNTHESIS;
D O I
10.1107/S1744309109022684
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
The crystal structure of PA1994 from Pseudomonas aeruginosa, a member of the Pfam PF06475 family classified as a domain of unknown function (DUF1089), reveals a novel fold comprising a 15-stranded beta-sheet wrapped around a single alpha-helix that assembles into a tight dimeric arrangement. The remote structural similarity to lipoprotein localization factors, in addition to the presence of an acidic pocket that is conserved in DUF1089 homologs, phospholipid-binding and sugar-binding proteins, indicate a role for PA1994 and the DUF1089 family in glycolipid metabolism. Genome-context analysis lends further support to the involvement of this family of proteins in glycolipid metabolism and indicates possible activation of DUF1089 homologs under conditions of bacterial cell-wall stress or host-pathogen interactions.
引用
收藏
页码:1211 / 1217
页数:7
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