1gwl: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
 
(One intermediate revision by the same user not shown)
Line 3: Line 3:
<StructureSection load='1gwl' size='340' side='right'caption='[[1gwl]], [[Resolution|resolution]] 1.51&Aring;' scene=''>
<StructureSection load='1gwl' size='340' side='right'caption='[[1gwl]], [[Resolution|resolution]] 1.51&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1gwl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pireq Pireq]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GWL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GWL FirstGlance]. <br>
<table><tr><td colspan='2'>[[1gwl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Piromyces_sp._'equi' Piromyces sp. 'equi']. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GWL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GWL FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</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]] 1.51&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1gwk|1gwk]], [[1gwm|1gwm]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</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=1gwl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gwl OCA], [https://pdbe.org/1gwl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gwl RCSB], [https://www.ebi.ac.uk/pdbsum/1gwl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gwl 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=1gwl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gwl OCA], [https://pdbe.org/1gwl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gwl RCSB], [https://www.ebi.ac.uk/pdbsum/1gwl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gwl ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/Q9C171_PIREQ Q9C171_PIREQ]
Carbohydrate-protein recognition is central to many biological processes. Enzymes that act on polysaccharide substrates frequently contain noncatalytic domains, "carbohydrate-binding modules" (CBMs), that target the enzyme to the appropriate substrate. CBMs that recognize specific plant structural polysaccharides are often able to accommodate both the variable backbone and the side-chain decorations of heterogeneous ligands. "CBM29" modules, derived from a noncatalytic component of the Piromyces equi cellulase/hemicellulase complex, provide an example of this selective yet flexible recognition. They discriminate strongly against some polysaccharides while remaining relatively promiscuous toward both beta-1,4-linked manno- and cello-oligosaccharides. This feature may reflect preferential, but flexible, targeting toward glucomannans in the plant cell wall. The three-dimensional structure of CBM29-2 and its complexes with cello- and mannohexaose reveal a beta-jelly-roll topology, with an extended binding groove on the concave surface. The orientation of the aromatic residues complements the conformation of the target sugar polymer while accommodation of both manno- and gluco-configured oligo- and polysaccharides is conferred by virtue of the plasticity of the direct interactions from their axial and equatorial 2-hydroxyls, respectively. Such flexible ligand recognition targets the anaerobic fungal complex to a range of different components in the plant cell wall and thus plays a pivotal role in the highly efficient degradation of this composite structure by the microbial eukaryote.
 
Promiscuity in ligand-binding: The three-dimensional structure of a Piromyces carbohydrate-binding module, CBM29-2, in complex with cello- and mannohexaose.,Charnock SJ, Bolam DN, Nurizzo D, Szabo L, McKie VA, Gilbert HJ, Davies GJ Proc Natl Acad Sci U S A. 2002 Oct 29;99(22):14077-82. Epub 2002 Oct 21. PMID:12391332<ref>PMID:12391332</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1gwl" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Pireq]]
[[Category: Piromyces sp. 'equi']]
[[Category: Charnock, S J]]
[[Category: Charnock SJ]]
[[Category: Davies, G J]]
[[Category: Davies GJ]]
[[Category: Nurizzo, D]]
[[Category: Nurizzo D]]
[[Category: Carbohydrate binding domain]]
[[Category: Cellohexaose]]
[[Category: Cellulosome]]
[[Category: Glucomannan]]
[[Category: Mannohexaose]]

Latest revision as of 06:28, 1 May 2024

Carbohydrate binding module family29 complexed with mannohexaose

1gwl, resolution 1.51Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1gwl&oldid=4135071"