1uu5: Difference between revisions
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New page: left|200px<br /> <applet load="1uu5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uu5, resolution 1.67Å" /> '''X-RAY CRYSTAL STRUC... |
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== | ==X-RAY CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMICOLA GRISEA CEL12A SOAKED WITH CELLOTETRAOSE== | ||
As part of an ongoing enzyme discovery program to investigate the | <StructureSection load='1uu5' size='340' side='right'caption='[[1uu5]], [[Resolution|resolution]] 1.67Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1uu5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Trichocladium_griseum Trichocladium griseum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UU5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UU5 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.67Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</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=1uu5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uu5 OCA], [https://pdbe.org/1uu5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uu5 RCSB], [https://www.ebi.ac.uk/pdbsum/1uu5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uu5 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q8NJY3_9PEZI Q8NJY3_9PEZI] | |||
== 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/uu/1uu5_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=1uu5 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
As part of an ongoing enzyme discovery program to investigate the properties and catalytic mechanism of glycoside hydrolase family 12 (GH 12) endoglucanases, a GH family that contains several cellulases that are of interest in industrial applications, we have solved four new crystal structures of wild-type Humicola grisea Cel12A in complexes formed by soaking with cellobiose, cellotetraose, cellopentaose, and a thio-linked cellotetraose derivative (G2SG2). These complex structures allow mapping of the non-covalent interactions between the enzyme and the glucosyl chain bound in subsites -4 to +2 of the enzyme, and shed light on the mechanism and function of GH 12 cellulases. The unhydrolysed cellopentaose and the G2SG2 cello-oligomers span the active site of the catalytically active H.grisea Cel12A enzyme, with the pyranoside bound in subsite -1 displaying a S31 skew boat conformation. After soaking in cellotetraose, the cello-oligomer that is found bound in site -4 to -1 contains a beta-1,3-linkage between the two cellobiose units in the oligomer, which is believed to have been formed by a transglycosylation reaction that has occurred during the ligand soak of the protein crystals. The close fit of this ligand and the binding sites occupied suggest a novel mixed beta-glucanase activity for this enzyme. | |||
Crystal complex structures reveal how substrate is bound in the -4 to the +2 binding sites of Humicola grisea Cel12A.,Sandgren M, Berglund GI, Shaw A, Stahlberg J, Kenne L, Desmet T, Mitchinson C J Mol Biol. 2004 Oct 1;342(5):1505-17. PMID:15364577<ref>PMID:15364577</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1uu5" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Glucanase 3D structures|Glucanase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Trichocladium griseum]] | |||
[[Category: Berglund GI]] | |||
[[Category: Driguez TH]] | |||
[[Category: Kenne L]] | |||
[[Category: Mitchinson C]] | |||
[[Category: Sandgren M]] | |||
[[Category: Shaw A]] | |||
[[Category: Stahlberg J]] | |||
