2ixa

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(New page: 200px<br /> <applet load="2ixa" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ixa, resolution 2.30&Aring;" /> '''A-ZYME, N-ACETYLGAL...)
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[[Image:2ixa.gif|left|200px]]<br />
 
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<applet load="2ixa" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2ixa, resolution 2.30&Aring;" />
 
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'''A-ZYME, N-ACETYLGALACTOSAMINIDASE'''<br />
 
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==About this Structure==
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==A-zyme, N-acetylgalactosaminidase==
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2IXA is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Flavobacterium_meningosepticum Flavobacterium meningosepticum]] with NAD, MRD and MPD as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.49 3.2.1.49]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2IXA OCA]].
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<StructureSection load='2ixa' size='340' side='right'caption='[[2ixa]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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[[Category: Flavobacterium meningosepticum]]
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== Structural highlights ==
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[[Category: Single protein]]
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<table><tr><td colspan='2'>[[2ixa]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Elizabethkingia_meningoseptica Elizabethkingia meningoseptica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IXA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IXA FirstGlance]. <br>
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[[Category: Bourne, Y.]]
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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[[Category: Clausen, H.]]
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>
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[[Category: Henrissat, B.]]
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ixa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ixa OCA], [https://pdbe.org/2ixa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ixa RCSB], [https://www.ebi.ac.uk/pdbsum/2ixa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ixa ProSAT]</span></td></tr>
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[[Category: Liu, Q.P.]]
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</table>
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[[Category: Sulzenbacher, G.]]
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== Function ==
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[[Category: MPD]]
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[https://www.uniprot.org/uniprot/GH109_ELIME GH109_ELIME]
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[[Category: MRD]]
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== Evolutionary Conservation ==
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[[Category: NAD]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: a-eco conversion]]
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Check<jmol>
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[[Category: hydrolase]]
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<jmolCheckbox>
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[[Category: n-acetylgalactosaminidase]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ix/2ixa_consurf.spt"</scriptWhenChecked>
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[[Category: nad]]
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=2ixa ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Enzymatic removal of blood group ABO antigens to develop universal red blood cells (RBCs) was a pioneering vision originally proposed more than 25 years ago. Although the feasibility of this approach was demonstrated in clinical trials for group B RBCs, a major obstacle in translating this technology to clinical practice has been the lack of efficient glycosidase enzymes. Here we report two bacterial glycosidase gene families that provide enzymes capable of efficient removal of A and B antigens at neutral pH with low consumption of recombinant enzymes. The crystal structure of a member of the alpha-N-acetylgalactosaminidase family reveals an unusual catalytic mechanism involving NAD+. The enzymatic conversion processes we describe hold promise for achieving the goal of producing universal RBCs, which would improve the blood supply while enhancing the safety of clinical transfusions.
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 19:57:38 2007''
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Bacterial glycosidases for the production of universal red blood cells.,Liu QP, Sulzenbacher G, Yuan H, Bennett EP, Pietz G, Saunders K, Spence J, Nudelman E, Levery SB, White T, Neveu JM, Lane WS, Bourne Y, Olsson ML, Henrissat B, Clausen H Nat Biotechnol. 2007 Apr;25(4):454-64. Epub 2007 Apr 1. PMID:17401360<ref>PMID:17401360</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2ixa" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Elizabethkingia meningoseptica]]
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[[Category: Large Structures]]
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[[Category: Bourne Y]]
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[[Category: Clausen H]]
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[[Category: Henrissat B]]
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[[Category: Liu QP]]
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[[Category: Sulzenbacher G]]

Current revision

A-zyme, N-acetylgalactosaminidase

PDB ID 2ixa

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