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2yb4

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Revision as of 03:22, 5 August 2016

Structure of an amidohydrolase from Chromobacterium violaceum (EFI target EFI-500202) with bound SO4, no metal

Structural highlights

2yb4 is a 1 chain structure with sequence from "chromobacterium_janthinum"_(zopf)_ford_1927 "chromobacterium janthinum" (zopf) ford 1927. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	2yb1
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

In bacteria, 3',5'-adenosine bisphosphate (pAp) is generated from 3'-phosphoadenosine 5'-phosphosulfate in the sulfate assimilation pathway, and from coenzyme A by the transfer of the phosphopantetheine group to the acyl-carrier protein. pAp is subsequently hydrolyzed to 5'-AMP and orthophosphate, and this reaction has been shown to be important for superoxide stress tolerance. Herein, we report the discovery of the first instance of an enzyme from the amidohydrolase superfamily that is capable of hydrolyzing pAp. Crystal structures of Cv1693 from Chromobacterium violaceum have been determined to a resolution of 1.9 A with AMP and orthophosphate bound in the active site. The enzyme has a trinuclear metal center in the active site with three Mn2+ ions. This enzyme (Cv1693) belongs to the Cluster of Orthologous Groups cog0613 from the polymerase and histidinol phosphatase family of enzymes. The values of kcat and kcat/Km for the hydrolysis of pAp are 22 s-1 and 1.4 x 106 M-1 s-1, respectively. The enzyme is promiscuous and is able to hydrolyze other 3',5'-bisphosphonucleotides (pGp, pCp, pUp, and pIp) and 2'-deoxynucleotides with comparable catalytic efficiency. The enzyme is capable of hydrolyzing short oligonucleotides (pdA)5, albeit at rates much lower than that of pAp. Enzymes from two other enzyme families have previously been found to hydrolyze pAp at physiologically significant rates. These enzymes include CysQ from Escherichia coli (cog1218) and YtqI/NrnA from Bacillus subtilis (cog0618). Identification of the functional homologues to the experimentally verified pAp phosphatases from cog0613, cog1218, and cog0618 suggests that there is relatively little overlap of enzymes with this function in sequenced bacterial genomes.

Prospecting for Unannotated Enzymes: Discovery of a 3',5'-Nucleotide Bisphosphate Phosphatase within the Amidohydrolase Superfamily.,Cummings JA, Vetting M, Ghodge SV, Xu C, Hillerich B, Seidel RD, Almo SC, Raushel FM Biochemistry. 2014 Jan 13. PMID:24401123^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Cummings JA, Vetting M, Ghodge SV, Xu C, Hillerich B, Seidel RD, Almo SC, Raushel FM. Prospecting for Unannotated Enzymes: Discovery of a 3',5'-Nucleotide Bisphosphate Phosphatase within the Amidohydrolase Superfamily. Biochemistry. 2014 Jan 13. PMID:24401123 doi:http://dx.doi.org/10.1021/bi401640r

1 Structural highlights
2 Publication Abstract from PubMed
3 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2yb4"

@@ Line 1: / Line 1: @@
 ==Structure of an amidohydrolase from Chromobacterium violaceum (EFI target EFI-500202) with bound SO4, no metal==
 <StructureSection load='2yb4' size='340' side='right' caption='[[2yb4]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2yb1|2yb1]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2yb4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yb4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2yb4 RCSB], [http://www.ebi.ac.uk/pdbsum/2yb4 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2yb4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yb4 OCA], [http://pdbe.org/2yb4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2yb4 RCSB], [http://www.ebi.ac.uk/pdbsum/2yb4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2yb4 ProSAT]</span></td></tr>
 </table>
 <div style="background-color:#fffaf0;">
@@ Line 15: / Line 16: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2yb4" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

2yb4

From Proteopedia

Revision as of 03:22, 5 August 2016

Structure of an amidohydrolase from Chromobacterium violaceum (EFI target EFI-500202) with bound SO4, no metal

Structural highlights

Publication Abstract from PubMed

References

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