2H1T

Crystal structure of a duf1089 family protein (pa1994) from pseudomonas aeruginosa at 1.80 A resolution

Summary for 2H1T

• Entry DOI: 10.2210/pdb2h1t/pdb
• Descriptor: Hypothetical protein, 1,2-ETHANEDIOL, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (4 entities in total)
• Functional Keywords: structural genomics, joint center for structural genomics, jcsg, protein structure initiative, psi-2, unknown function
• Biological source: Pseudomonas aeruginosa
• Total number of polymer chains: 2
• Total formula weight: 44270.81

Authors

Joint Center for Structural Genomics (JCSG) (deposition date: 2006-05-16, release date: 2006-05-30, Last modification date: 2024-11-20)

Primary citation

Bakolitsa, C.,Kumar, A.,McMullan, D.,Krishna, S.S.,Miller, M.D.,Carlton, D.,Najmanovich, R.,Abdubek, P.,Astakhova, T.,Chiu, H.J.,Clayton, T.,Deller, M.C.,Duan, L.,Elias, Y.,Feuerhelm, J.,Grant, J.C.,Grzechnik, S.K.,Han, G.W.,Jaroszewski, L.,Jin, K.K.,Klock, H.E.,Knuth, M.W.,Kozbial, P.,Marciano, D.,Morse, A.T.,Nigoghossian, E.,Okach, L.,Oommachen, S.,Paulsen, J.,Reyes, R.,Rife, C.L.,Trout, C.V.,van den Bedem, H.,Weekes, D.,White, A.,Xu, Q.,Hodgson, K.O.,Wooley, J.,Elsliger, M.A.,Deacon, A.M.,Godzik, A.,Lesley, S.A.,Wilson, I.A.
The structure of the first representative of Pfam family PF06475 reveals a new fold with possible involvement in glycolipid metabolism.
Acta Crystallogr.,Sect.F, 66:1211-1217, 2010

PubMed Abstract: 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 β-sheet wrapped around a single α-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.

PubMed: 20944213
DOI: 10.1107/S1744309109022684

Experimental method

X-RAY DIFFRACTION (1.8 Å)