1m7j: Difference between revisions

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 <StructureSection load='1m7j' size='340' side='right'caption='[[1m7j]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1m7j]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Alcfa Alcfa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M7J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M7J FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1m7j]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Alcaligenes_faecalis Alcaligenes faecalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M7J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M7J FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</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]] 1.5&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/N-acyl-D-amino-acid_deacylase N-acyl-D-amino-acid deacylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.81 3.5.1.81] </span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=1m7j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m7j OCA], [https://pdbe.org/1m7j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m7j RCSB], [https://www.ebi.ac.uk/pdbsum/1m7j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m7j ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q9AGH8_ALCFA Q9AGH8_ALCFA]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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 </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1m7j ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-D-Aminoacylase is an attractive candidate for commercial production of D-amino acids through its catalysis in the hydrolysis of N-acyl-D-amino acids. We report here the first D-aminoacylase crystal structure from A. faecalis at 1.5-A resolution. The protein comprises a small beta-barrel, and a catalytic (betaalpha)(8)-barrel with a 63-residue insertion. The enzyme structure shares significant similarity to the alpha/beta-barrel amidohydrolase superfamily, in which the beta-strands in both barrels superimpose well. Unexpectedly, the enzyme binds two zinc ions with widely different affinities, although only the tightly bound zinc ion is required for activity. One zinc ion is coordinated by Cys(96), His(220), and His(250), while the other is loosely chelated by His(67), His(69), and Cys(96). This is the first example of the metal ion coordination by a cysteine residue in the superfamily. Therefore, D-aminoacylase defines a novel subset and is a mononuclear zinc metalloenzyme but containing a binuclear active site. The preferred substrate was modeled into a hydrophobic pocket, revealing the substrate specificity and enzyme catalysis. The 63-residue insertion containing substrate-interacting residues may act as a gate controlling access to the active site, revealing that the substrate binding would induce a closed conformation to sequester the catalysis from solvent.
-Crystal structure of D-aminoacylase from Alcaligenes faecalis DA1. A novel subset of amidohydrolases and insights into the enzyme mechanism.,Liaw SH, Chen SJ, Ko TP, Hsu CS, Chen CJ, Wang AH, Tsai YC J Biol Chem. 2003 Feb 14;278(7):4957-62. Epub 2002 Nov 25. PMID:12454005<ref>PMID:12454005</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1m7j" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Aminoacylase 3D structures|Aminoacylase 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Alcfa]]
+[[Category: Alcaligenes faecalis]]
 [[Category: Large Structures]]
-[[Category: N-acyl-D-amino-acid deacylase]]
+[[Category: Chen S-J]]
-[[Category: Chen, S J]]
+[[Category: Hsu C-S]]
-[[Category: Hsu, C S]]
+[[Category: Ko T-P]]
-[[Category: Ko, T P]]
+[[Category: Liaw S-H]]
-[[Category: Liaw, S H]]
+[[Category: Tsai Y-C]]
-[[Category: Tsai, Y C]]
+[[Category: Wang AH-J]]
-[[Category: Wang, A H.J]]
-[[Category: Hydrolase]]
-[[Category: Metal-dependent amidohydrolase]]
-[[Category: Tin-barrel]]