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3e74

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Revision as of 09:04, 25 October 2017

Crystal structure of E. coli allantoinase with iron ions at the metal center

Structural highlights

3e74 is a 4 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:	,
Related:	3e75
Gene:	allB, glxB3, ybbX, b0512, JW0500 (ECOLI)
Activity:	Allantoinase, with EC number 3.5.2.5
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ALLB_ECOLI] Catalyzes the conversion of allantoin (5-ureidohydantoin) to allantoic acid by hydrolytic cleavage of the five-member hydantoin ring.^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Allantoinase acts as a key enzyme for the biogenesis and degradation of ureides by catalyzing the conversion of (S)-allantoin into allantoate, the final step in the ureide pathway. Despite limited sequence similarity, biochemical studies of the enzyme suggested that allantoinase belongs to the amidohydrolase family. In this study, the crystal structure of allantoinase from Escherichia coli was determined at 2.1 A resolution. The enzyme consists of a homotetramer in which each monomer contains two domains: a pseudo-triosephosphate-isomerase barrel and a beta-sheet. Analogous to other enzymes in the amidohydrolase family, allantoinase retains a binuclear metal center in the active site, embedded within the barrel fold. Structural analyses demonstrated that the metal ions in the active site ligate one hydroxide and six residues that are conserved among allantoinases from other organisms. Functional analyses showed that the presence of zinc in the metal center is essential for catalysis and enantioselectivity of substrate. Both the metal center and active site residues Asn94 and Ser317 play crucial roles in dictating enzyme activity. These structural and functional features are distinctively different from those of the metal-independent allantoinase, which was very recently identified.

Crystal structure of metal-dependent allantoinase from Escherichia coli.,Kim K, Kim MI, Chung J, Ahn JH, Rhee S J Mol Biol. 2009 Apr 17;387(5):1067-74. Epub 2009 Feb 24. PMID:19248789^[3]

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

References

↑ Cusa E, Obradors N, Baldoma L, Badia J, Aguilar J. Genetic analysis of a chromosomal region containing genes required for assimilation of allantoin nitrogen and linked glyoxylate metabolism in Escherichia coli. J Bacteriol. 1999 Dec;181(24):7479-84. PMID:10601204
↑ Kim GJ, Lee DE, Kim HS. Functional expression and characterization of the two cyclic amidohydrolase enzymes, allantoinase and a novel phenylhydantoinase, from Escherichia coli. J Bacteriol. 2000 Dec;182(24):7021-8. PMID:11092864
↑ Kim K, Kim MI, Chung J, Ahn JH, Rhee S. Crystal structure of metal-dependent allantoinase from Escherichia coli. J Mol Biol. 2009 Apr 17;387(5):1067-74. Epub 2009 Feb 24. PMID:19248789 doi:10.1016/j.jmb.2009.02.041

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3e74"

@@ Line 1: / Line 1: @@
 ==Crystal structure of E. coli allantoinase with iron ions at the metal center==
 <StructureSection load='3e74' size='340' side='right' caption='[[3e74]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
@@ Line 8: / Line 9: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">allB, glxB3, ybbX, b0512, JW0500 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Allantoinase Allantoinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.5 3.5.2.5] </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=3e74 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e74 OCA], [http://pdbe.org/3e74 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3e74 RCSB], [http://www.ebi.ac.uk/pdbsum/3e74 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=3e74 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e74 OCA], [http://pdbe.org/3e74 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3e74 RCSB], [http://www.ebi.ac.uk/pdbsum/3e74 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3e74 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 42: / Line 43: @@
 [[Category: Purine metabolism]]
 [[Category: Small beta-sheet domain]]
+[[Category: Zinc]]

3e74

From Proteopedia

Revision as of 09:04, 25 October 2017

Crystal structure of E. coli allantoinase with iron ions at the metal center

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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