3mdu: Difference between revisions

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 <StructureSection load='3mdu' size='340' side='right'caption='[[3mdu]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3mdu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MDU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MDU FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3mdu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MDU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MDU FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NGQ:N-CARBAMIMIDOYL-L-GLUTAMIC+ACID'>NGQ</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4003&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3mdw|3mdw]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NGQ:N-CARBAMIMIDOYL-L-GLUTAMIC+ACID'>NGQ</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PA5106 ([https://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'>[https://proteopedia.org/fgij/fg.htm?mol=3mdu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mdu OCA], [https://pdbe.org/3mdu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mdu RCSB], [https://www.ebi.ac.uk/pdbsum/3mdu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mdu ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[https://www.uniprot.org/uniprot/HUTF_PSEAE HUTF_PSEAE] Catalyzes the hydrolysis of N-formimino-L-glutamate to N-formyl-L-glutamate and ammonia.<ref>PMID:16475788</ref> <ref>PMID:17128965</ref>
-N-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<ref>PMID:25559274</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3mdu" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
@@ Line 23: / Line 15: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Almo, S C]]
+[[Category: Pseudomonas aeruginosa]]
-[[Category: Fedorov, A A]]
+[[Category: Almo SC]]
-[[Category: Fedorov, E V]]
+[[Category: Fedorov AA]]
-[[Category: Marti-Arbona, R]]
+[[Category: Fedorov EV]]
-[[Category: Raushel, F M]]
+[[Category: Marti-Arbona R]]
-[[Category: Amonohydralase family]]
+[[Category: Raushel FM]]
-[[Category: Hydrolase]]
-[[Category: N-formimino-l-glutamate iminohydrolase]]
-[[Category: N-guanidino-l-glutamate]]