3L5O

Crystal structure of protein with unknown function from DUF364 family (ZP_00559375.1) from Desulfitobacterium hafniense DCB-2 at 2.01 A resolution

Replaces:  2H1Q

Summary for 3L5O

• Entry DOI: 10.2210/pdb3l5o/pdb
• Descriptor: uncharacterized protein from DUF364 family, CHLORIDE ION, IMIDAZOLE, ... (5 entities in total)
• Functional Keywords: rare metals, siderophores, adenosyl binding site, protein with unknown function from duf364 family, structural genomics, joint center for structural genomics, jcsg, protein structure initiative, psi-2, adenosyl binding protein
• Biological source: Desulfitobacterium hafniense
• Total number of polymer chains: 2
• Total formula weight: 61645.10

Authors

Joint Center for Structural Genomics,Joint Center for Structural Genomics (JCSG) (deposition date: 2009-12-22, release date: 2010-02-02, Last modification date: 2024-11-06)

Primary citation

Miller, M.D.,Aravind, L.,Bakolitsa, C.,Rife, C.L.,Carlton, 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.,Kozbial, P.,Krishna, S.S.,Kumar, A.,Marciano, D.,McMullan, D.,Morse, A.T.,Nigoghossian, E.,Okach, L.,Reyes, R.,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.
Structure of the first representative of Pfam family PF04016 (DUF364) reveals enolase and Rossmann-like folds that combine to form a unique active site with a possible role in heavy-metal chelation.
Acta Crystallogr.,Sect.F, 66:1167-1173, 2010

PubMed Abstract: The crystal structure of Dhaf4260 from Desulfitobacterium hafniense DCB-2 was determined by single-wavelength anomalous diffraction (SAD) to a resolution of 2.01 Å using the semi-automated high-throughput pipeline of the Joint Center for Structural Genomics (JCSG) as part of the NIGMS Protein Structure Initiative (PSI). This protein structure is the first representative of the PF04016 (DUF364) Pfam family and reveals a novel combination of two well known domains (an enolase N-terminal-like fold followed by a Rossmann-like domain). Structural and bioinformatic analyses reveal partial similarities to Rossmann-like methyltransferases, with residues from the enolase-like fold combining to form a unique active site that is likely to be involved in the condensation or hydrolysis of molecules implicated in the synthesis of flavins, pterins or other siderophores. The genome context of Dhaf4260 and homologs additionally supports a role in heavy-metal chelation.

PubMed: 20944207
DOI: 10.1107/S1744309110007517

Experimental method

X-RAY DIFFRACTION (2.01 Å)