1fcv: Difference between revisions

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 <StructureSection load='1fcv' size='340' side='right'caption='[[1fcv]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1fcv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Apime Apime]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FCV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FCV FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1fcv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Apis_mellifera Apis mellifera]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FCV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FCV FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GCU:D-GLUCURONIC+ACID'>GCU</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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]] 2.65&#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;'>[[1fcq|1fcq]], [[1fcu|1fcu]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GCU:D-GLUCURONIC+ACID'>GCU</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.35 3.2.1.35] </span></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=1fcv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fcv OCA], [https://pdbe.org/1fcv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fcv RCSB], [https://www.ebi.ac.uk/pdbsum/1fcv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fcv ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/HUGA_APIME HUGA_APIME]] Hydrolyzes high molecular weight hyaluronic acid to produce small oligosaccharides (By similarity).
+[https://www.uniprot.org/uniprot/HUGA_APIME HUGA_APIME] Hydrolyzes high molecular weight hyaluronic acid to produce small oligosaccharides (By similarity).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 21: / Line 20: @@
 </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=1fcv ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-BACKGROUND: Hyaluronic acid (HA) is the most abundant glycosaminoglycan of vertebrate extracellular spaces and is specifically degraded by a beta-1,4 glycosidase. Bee venom hyaluronidase (Hya) shares 30% sequence identity with human hyaluronidases, which are involved in fertilization and the turnover of HA. On the basis of sequence similarity, mammalian enzymes and Hya are assigned to glycosidase family 56 for which no structure has been reported yet. RESULTS: The crystal structure of recombinant (Baculovirus) Hya was determined at 1.6 A resolution. The overall topology resembles a classical (beta/alpha)(8) TIM barrel except that the barrel is composed of only seven strands. A long substrate binding groove extends across the C-terminal end of the barrel. Cocrystallization with a substrate analog revealed the presence of a HA tetramer bound to subsites -4 to -1 and distortion of the -1 sugar. CONCLUSIONS: The structure of the complex strongly suggest an acid-base catalytic mechanism, in which Glu113 acts as the proton donor and the N-acetyl group of the substrate is the nucleophile. The location of the catalytic residues shows striking similarity to bacterial chitinase which also operates via a substrate-assisted mechanism.
-Crystal structure of hyaluronidase, a major allergen of bee venom.,Markovic-Housley Z, Miglierini G, Soldatova L, Rizkallah PJ, Muller U, Schirmer T Structure. 2000 Oct 15;8(10):1025-35. PMID:11080624<ref>PMID:11080624</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1fcv" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Hyaluronidase 3D structures|Hyaluronidase 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Apime]]
+[[Category: Apis mellifera]]
-[[Category: Hydrolase]]
 [[Category: Large Structures]]
-[[Category: Markovic-Housley, Z]]
+[[Category: Markovic-Housley Z]]
-[[Category: Miglierini, G]]
+[[Category: Miglierini G]]
-[[Category: Mueller, U]]
+[[Category: Mueller U]]
-[[Category: Rizkallah, P J]]
+[[Category: Rizkallah PJ]]
-[[Category: Schirmer, T]]
+[[Category: Schirmer T]]
-[[Category: Soldatova, L]]
+[[Category: Soldatova L]]
-[[Category: Stranded tim barrel]]
-[[Category: Allergen]]
-[[Category: Glycosidase family 56]]
-[[Category: Hyaluronic acid]]