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1y65

From Proteopedia

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(New page: 200px<br /><applet load="1y65" size="450" color="white" frame="true" align="right" spinBox="true" caption="1y65, resolution 1.850&Aring;" /> '''Crystal structure o...)
Current revision (06:53, 23 August 2023) (edit) (undo)
 
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[[Image:1y65.gif|left|200px]]<br /><applet load="1y65" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1y65, resolution 1.850&Aring;" />
 
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'''Crystal structure of beta-hexosaminidase from Vibrio cholerae in complex with N-acetyl-D-glucosamine to a resolution of 1.85'''<br />
 
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==About this Structure==
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==Crystal structure of beta-hexosaminidase from Vibrio cholerae in complex with N-acetyl-D-glucosamine to a resolution of 1.85==
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1Y65 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae] with NAG as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Beta-N-acetylhexosaminidase Beta-N-acetylhexosaminidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.52 3.2.1.52] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Y65 OCA].
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<StructureSection load='1y65' size='340' side='right'caption='[[1y65]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
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[[Category: Beta-N-acetylhexosaminidase]]
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== Structural highlights ==
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[[Category: Single protein]]
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<table><tr><td colspan='2'>[[1y65]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y65 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y65 FirstGlance]. <br>
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[[Category: Vibrio cholerae]]
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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]] 1.85&#8491;</td></tr>
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[[Category: Burley, S.K.]]
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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[[Category: Gorman, J.]]
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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=1y65 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y65 OCA], [https://pdbe.org/1y65 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y65 RCSB], [https://www.ebi.ac.uk/pdbsum/1y65 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y65 ProSAT], [https://www.topsan.org/Proteins/NYSGXRC/1y65 TOPSAN]</span></td></tr>
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[[Category: NYSGXRC, New.York.Structural.GenomiX.Research.Consortium.]]
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</table>
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[[Category: Shapiro, L.]]
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== Function ==
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[[Category: NAG]]
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[https://www.uniprot.org/uniprot/NAGZ_VIBCH NAGZ_VIBCH] Plays a role in peptidoglycan recycling by cleaving the terminal beta-1,4-linked N-acetylglucosamine (GlcNAc) from peptide-linked peptidoglycan fragments, giving rise to free GlcNAc, anhydro-N-acetylmuramic acid and anhydro-N-acetylmuramic acid-linked peptides. Plays a role in beta-lactam antibiotic resistance via its role in generating anhydro-N-acetylmuramic acid-linked peptides; these peptides function as signaling molecules that induce high-level expression of the beta-lactamase AmpC.<ref>PMID:24009110</ref> <ref>PMID:17439950</ref> <ref>PMID:19499593</ref>
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[[Category: beta-alpha barrel]]
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== Evolutionary Conservation ==
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[[Category: new york structural genomix research consortium]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: nysgxrc]]
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Check<jmol>
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[[Category: protein structure initiative]]
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<jmolCheckbox>
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[[Category: psi]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/y6/1y65_consurf.spt"</scriptWhenChecked>
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[[Category: structural genomics]]
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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=1y65 ConSurf].
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<div style="clear:both"></div>
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:35:47 2007''
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==See Also==
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*[[Beta-Hexosaminidase|Beta-Hexosaminidase]]
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*[[Beta-Hexosaminidase 3D structures|Beta-Hexosaminidase 3D structures]]
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*[[Beta-N-acetylhexosaminidase 3D structures|Beta-N-acetylhexosaminidase 3D structures]]
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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: Large Structures]]
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[[Category: Vibrio cholerae]]
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[[Category: Burley SK]]
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[[Category: Gorman J]]
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[[Category: Shapiro L]]

Current revision

Crystal structure of beta-hexosaminidase from Vibrio cholerae in complex with N-acetyl-D-glucosamine to a resolution of 1.85

PDB ID 1y65

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