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==The structure of N-formimino-L-Glutamate Iminohydrolase from Pseudomonas aeruginosa complexed with N-Guanidino-L-Glutamate== | ==The structure of N-formimino-L-Glutamate Iminohydrolase from Pseudomonas aeruginosa complexed with N-Guanidino-L-Glutamate== | ||
<StructureSection load='3mdu' size='340' side='right' caption='[[3mdu]], [[Resolution|resolution]] 1.40Å' scene=''> | <StructureSection load='3mdu' size='340' side='right' caption='[[3mdu]], [[Resolution|resolution]] 1.40Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3mdw|3mdw]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3mdw|3mdw]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PA5106 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PA5106 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885])</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=3mdu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mdu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mdu RCSB], [http://www.ebi.ac.uk/pdbsum/3mdu 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=3mdu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mdu OCA], [http://pdbe.org/3mdu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3mdu RCSB], [http://www.ebi.ac.uk/pdbsum/3mdu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3mdu ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3mdu" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 06:55, 10 December 2016
The structure of N-formimino-L-Glutamate Iminohydrolase from Pseudomonas aeruginosa complexed with N-Guanidino-L-GlutamateThe structure of N-formimino-L-Glutamate Iminohydrolase from Pseudomonas aeruginosa complexed with N-Guanidino-L-Glutamate
Structural highlights
Publication Abstract from PubMedN-Formimino-l-glutamate iminohydrolase (HutF), from Pseudomonas aeruginosa with a locus tag of Pa5106 ( gi|15600299 ), is a member of the amidohydrolase superfamily. This enzyme catalyzes the deamination of N-formimino-l-glutamate to N-formyl-l-glutamate and ammonia in the histidine degradation pathway. The crystal structure of Pa5106 was determined in the presence of the inhibitors N-formimino-l-aspartate and N-guanidino-l-glutaric acid at resolutions of 1.9 and 1.4 A, respectively. The structure of an individual subunit is composed of two domains with the larger domain folding as a distorted (beta/alpha)8-barrel. The (beta/alpha)8-barrel domain is composed of eight beta-strands flanked by 11 alpha-helices, whereas the smaller domain is made up of eight beta-strands. The active site of Pa5106 contains a single zinc atom that is coordinated by His-56, His-58, His-232, and Asp-320. The nucleophilic solvent water molecule coordinates with the zinc atom at a distance of 2.0 A and is hydrogen bonded to Asp-320 and His-269. The alpha-carboxylate groups of both inhibitors are hydrogen bonded to the imidazole moiety of His-206, the hydroxyl group of Tyr-121, and the side chain amide group of Gln-61. The side chain carboxylate groups of the two inhibitors are ion-paired with the guanidino groups of Arg-209 and Arg-82. Computational docking of high-energy tetrahedral intermediate forms of the substrate, N-formimino-l-glutamate, to the three-dimensional structure of Pa5106 suggests that this compound likely undergoes a re-faced nucleophilic attack at the formimino group by the metal-bound hydroxide. A catalytic mechanism of the reaction catalyzed by Pa5106 is proposed. Structure of N-Formimino-l-glutamate Iminohydrolase from Pseudomonas aeruginosa.,Fedorov AA, Marti-Arbona R, Nemmara VV, Hitchcock D, Fedorov EV, Almo SC, Raushel FM Biochemistry. 2015 Jan 16. PMID:25559274[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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