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<StructureSection load='1jop' size='340' side='right'caption='[[1jop]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
<StructureSection load='1jop' size='340' side='right'caption='[[1jop]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1jop]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacterium_influenzae"_lehmann_and_neumann_1896 "bacterium influenzae" lehmann and neumann 1896]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JOP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JOP FirstGlance]. <br>
<table><tr><td colspan='2'>[[1jop]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JOP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JOP FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</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]] 2.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</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=1jop FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jop OCA], [https://pdbe.org/1jop PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jop RCSB], [https://www.ebi.ac.uk/pdbsum/1jop PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jop ProSAT]</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=1jop FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jop OCA], [https://pdbe.org/1jop PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jop RCSB], [https://www.ebi.ac.uk/pdbsum/1jop PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jop ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NANQ_HAEIN NANQ_HAEIN] Opens both the alpha- and beta-forms of N-acetylneuraminate (sialic acid; Neu5Ac) to provide aceneuramate, the preferred substrate for NanA (Probable). Has preferential activity on the beta-anomer rather than the alpha-anomer. Accelerates a reaction that is spontaneous at slightly alkaline pH, facilitates the reaction at acidic pH (By similarity).[UniProtKB:P45424]<ref>PMID:33895133</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[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=1jop ConSurf].
</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=1jop ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The yhcH gene is part of the nan operon in bacteria that encodes proteins involved in sialic acid catabolism. Determination of the crystal structure of YhcH from Haemophilus influenzae was undertaken as part of a structural genomics effort in order to assist with the functional assignment of the protein. The structure was determined at 2.2-A resolution by multiple-wavelength anomalous diffraction. The protein fold is a variation of the double-stranded beta-helix. Two antiparallel beta-sheets form a funnel opened at one side, where a putative active site contains a copper ion coordinated to the side chains of two histidine and two carboxylic acid residues. A comparison to other proteins with a similar fold and analysis of the genomic context suggested that YhcH may be a sugar isomerase involved in processing of exogenous sialic acid.
Crystal structure of the bacterial YhcH protein indicates a role in sialic acid catabolism.,Teplyakov A, Obmolova G, Toedt J, Galperin MY, Gilliland GL J Bacteriol. 2005 Aug;187(16):5520-7. PMID:16077096<ref>PMID:16077096</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1jop" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacterium influenzae lehmann and neumann 1896]]
[[Category: Haemophilus influenzae]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Gilliland, G L]]
[[Category: Gilliland GL]]
[[Category: Obmolova, G]]
[[Category: Obmolova G]]
[[Category: S2F, Structure 2.Function Project]]
[[Category: Teplyakov A]]
[[Category: Teplyakov, A]]
[[Category: Beta-sandwich]]
[[Category: S2f]]
[[Category: Structural genomic]]
[[Category: Structure 2 function project]]
[[Category: Unknown function]]

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