3IRB
Crystal structure of protein with unknown function from DUF35 family (13815350) from SULFOLOBUS SOLFATARICUS at 1.80 A resolution
Replaces: 2GNRSummary for 3IRB
| Entry DOI | 10.2210/pdb3irb/pdb |
| Descriptor | uncharacterized protein from DUF35 family, ZINC ION, SULFATE ION, ... (5 entities in total) |
| Functional Keywords | 13815350, protein with unknown function from duf35 family, structural genomics, joint center for structural genomics, jcsg, protein structure initiative, psi-2, domain of unknown function duf35, unknown function, acyl-coa binding protein |
| Biological source | Sulfolobus solfataricus (Archaea) |
| Total number of polymer chains | 2 |
| Total formula weight | 34102.69 |
| Authors | Joint Center for Structural Genomics (JCSG) (deposition date: 2009-08-21, release date: 2009-09-01, Last modification date: 2024-11-06) |
| Primary citation | Krishna, S.S.,Aravind, L.,Bakolitsa, C.,Caruthers, J.,Carlton, D.,Miller, M.D.,Abdubek, P.,Astakhova, T.,Axelrod, H.L.,Chiu, H.J.,Clayton, T.,Deller, M.C.,Duan, L.,Feuerhelm, J.,Grant, J.C.,Han, G.W.,Jaroszewski, L.,Jin, K.K.,Klock, H.E.,Knuth, M.W.,Kumar, A.,Marciano, D.,McMullan, D.,Morse, A.T.,Nigoghossian, E.,Okach, L.,Reyes, R.,Rife, C.L.,van den Bedem, H.,Weekes, D.,Xu, Q.,Hodgson, K.O.,Wooley, J.,Elsliger, M.A.,Deacon, A.M.,Godzik, A.,Lesley, S.A.,Wilson, I.A. The structure of SSO2064, the first representative of Pfam family PF01796, reveals a novel two-domain zinc-ribbon OB-fold architecture with a potential acyl-CoA-binding role. Acta Crystallogr.,Sect.F, 66:1160-1166, 2010 Cited by PubMed Abstract: SSO2064 is the first structural representative of PF01796 (DUF35), a large prokaryotic family with a wide phylogenetic distribution. The structure reveals a novel two-domain architecture comprising an N-terminal, rubredoxin-like, zinc ribbon and a C-terminal, oligonucleotide/oligosaccharide-binding (OB) fold domain. Additional N-terminal helical segments may be involved in protein-protein interactions. Domain architectures, genomic context analysis and functional evidence from certain bacterial representatives of this family suggest that these proteins form a novel fatty-acid-binding component that is involved in the biosynthesis of lipids and polyketide antibiotics and that they possibly function as acyl-CoA-binding proteins. This structure has led to a re-evaluation of the DUF35 family, which has now been split into two entries in the latest Pfam release (v.24.0). PubMed: 20944206DOI: 10.1107/S1744309110002514 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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