1tr9: Difference between revisions

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[[Image:1tr9.png|left|200px]]


{{STRUCTURE_1tr9|  PDB=1tr9  |  SCENE=  }}
==Structure of beta-hexosaminidase from Vibrio cholerae==
 
<StructureSection load='1tr9' size='340' side='right'caption='[[1tr9]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
===Structure of beta-hexosaminidase from Vibrio cholerae===
== Structural highlights ==
 
<table><tr><td colspan='2'>[[1tr9]] 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=1TR9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TR9 FirstGlance]. <br>
{{ABSTRACT_PUBMED_016300407}}
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
==About this Structure==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1tr9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tr9 OCA], [https://pdbe.org/1tr9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tr9 RCSB], [https://www.ebi.ac.uk/pdbsum/1tr9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tr9 ProSAT], [https://www.topsan.org/Proteins/NYSGXRC/1tr9 TOPSAN]</span></td></tr>
[[1tr9]] is a 1 chain structure of [[Beta-Hexosaminidase]] with sequence from [http://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TR9 OCA].  
</table>
== Function ==
[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>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tr/1tr9_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1tr9 ConSurf].
<div style="clear:both"></div>


==See Also==
==See Also==
*[[Beta-Hexosaminidase|Beta-Hexosaminidase]]
*[[Beta-Hexosaminidase|Beta-Hexosaminidase]]
 
*[[Beta-Hexosaminidase 3D structures|Beta-Hexosaminidase 3D structures]]
==Reference==
*[[Beta-N-acetylhexosaminidase 3D structures|Beta-N-acetylhexosaminidase 3D structures]]
<ref group="xtra">PMID:016300407</ref><ref group="xtra">PMID:016342944</ref><references group="xtra"/>
== References ==
[[Category: Beta-N-acetylhexosaminidase]]
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Vibrio cholerae]]
[[Category: Vibrio cholerae]]
[[Category: Burley, S K.]]
[[Category: Burley SK]]
[[Category: Gorman, J.]]
[[Category: Gorman J]]
[[Category: NYSGXRC, New York SGX Research Center for Structural Genomics.]]
[[Category: Shapiro L]]
[[Category: Shapiro, L.]]
[[Category: Beta-alpha barrel]]
[[Category: Beta-hexosaminidase]]
[[Category: Hydrolase]]
[[Category: New york sgx research center for structural genomic]]
[[Category: Nysgxrc]]
[[Category: Protein structure initiative]]
[[Category: Psi]]
[[Category: Structural genomic]]

Latest revision as of 07:55, 17 October 2024

Structure of beta-hexosaminidase from Vibrio choleraeStructure of beta-hexosaminidase from Vibrio cholerae

Structural highlights

1tr9 is a 1 chain structure with sequence from Vibrio cholerae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

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.[1] [2] [3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Stubbs KA, Bacik JP, Perley-Robertson GE, Whitworth GE, Gloster TM, Vocadlo DJ, Mark BL. The Development of Selective Inhibitors of NagZ: Increased Susceptibility of Gram-Negative Bacteria to beta-Lactams. Chembiochem. 2013 Oct 11;14(15):1973-81. doi: 10.1002/cbic.201300395. Epub 2013, Sep 5. PMID:24009110 doi:http://dx.doi.org/10.1002/cbic.201300395
  2. ↑ Stubbs KA, Balcewich M, Mark BL, Vocadlo DJ. Small molecule inhibitors of a glycoside hydrolase attenuate inducible AmpC-mediated beta-lactam resistance. J Biol Chem. 2007 Jul 20;282(29):21382-91. Epub 2007 Apr 16. PMID:17439950 doi:10.1074/jbc.M700084200
  3. ↑ Balcewich MD, Stubbs KA, He Y, James TW, Davies GJ, Vocadlo DJ, Mark BL. Insight into a strategy for attenuating AmpC-mediated beta-lactam resistance: Structural basis for selective inhibition of the glycoside hydrolase NagZ. Protein Sci. 2009 Apr 16. PMID:19499593 doi:10.1002/pro.137

1tr9, resolution 1.80Å

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