2j1e: Difference between revisions

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<StructureSection load='2j1e' size='340' side='right'caption='[[2j1e]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='2j1e' size='340' side='right'caption='[[2j1e]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2j1e]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Clop1 Clop1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J1E OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2J1E FirstGlance]. <br>
<table><tr><td colspan='2'>[[2j1e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Clop1 Clop1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J1E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J1E FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2cbi|2cbi]], [[2cbj|2cbj]], [[2j1a|2j1a]], [[2j1f|2j1f]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2cbi|2cbi]], [[2cbj|2cbj]], [[2j1a|2j1a]], [[2j1f|2j1f]]</div></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2j1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j1e OCA], [http://pdbe.org/2j1e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2j1e RCSB], [http://www.ebi.ac.uk/pdbsum/2j1e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2j1e 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=2j1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j1e OCA], [https://pdbe.org/2j1e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j1e RCSB], [https://www.ebi.ac.uk/pdbsum/2j1e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j1e ProSAT]</span></td></tr>
</table>
</table>
== Evolutionary Conservation ==
== Evolutionary Conservation ==

Revision as of 10:58, 19 January 2022

High Resolution Crystal Structure of CBM32 from a N-acetyl-beta- hexosaminidase in complex with lacNAcHigh Resolution Crystal Structure of CBM32 from a N-acetyl-beta- hexosaminidase in complex with lacNAc

Structural highlights

2j1e is a 1 chain structure with sequence from Clop1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Evolutionary Conservation

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

Publication Abstract from PubMed

Clostridium perfringens is a notable colonizer of the human gastrointestinal tract. This bacterium is quite remarkable for a human pathogen by the number of glycoside hydrolases found in its genome. The modularity of these enzymes is striking as is the frequent occurrence of modules having amino acid sequence identity with family 32 carbohydrate-binding modules (CBMs), often referred to as F5/8 domains. Here we report the properties of family 32 CBMs from a C. perfringens N-acetyl-beta-hexosaminidase. Macroarray, UV difference, and isothermal titration calorimetry binding studies indicate a preference for the disaccharide LacNAc (beta-d-galactosyl-1,4-beta-d-N-acetylglucosamine). The molecular details of the interaction of this CBM with galactose, LacNAc, and the type II blood group H-trisaccharide are revealed by x-ray crystallographic studies at resolutions of 1.49, 2.4, and 2.3 A, respectively.

The interaction of a carbohydrate-binding module from a Clostridium perfringens N-acetyl-beta-hexosaminidase with its carbohydrate receptor.,Ficko-Blean E, Boraston AB J Biol Chem. 2006 Dec 8;281(49):37748-57. Epub 2006 Sep 21. PMID:16990278[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Ficko-Blean E, Boraston AB. The interaction of a carbohydrate-binding module from a Clostridium perfringens N-acetyl-beta-hexosaminidase with its carbohydrate receptor. J Biol Chem. 2006 Dec 8;281(49):37748-57. Epub 2006 Sep 21. PMID:16990278 doi:10.1074/jbc.M606126200

2j1e, resolution 2.40Å

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OCA