3amp: Difference between revisions
New page: '''Unreleased structure''' The entry 3amp is ON HOLD Authors: Cheng, Y.-S., Ko, T.-P., Liu, J.-R., Guo, R.-T. Description: crystal structure of cellulase 12A from Thermotoga maritima ... |
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==E134C-Cellotetraose complex of cellulase 12A from thermotoga maritima== | |||
<StructureSection load='3amp' size='340' side='right'caption='[[3amp]], [[Resolution|resolution]] 1.78Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3amp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AMP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AMP 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]] 1.78Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900005:beta-cellobiose'>PRD_900005</scene>, <scene name='pdbligand=PRD_900014:alpha-cellotriose'>PRD_900014</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=3amp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3amp OCA], [https://pdbe.org/3amp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3amp RCSB], [https://www.ebi.ac.uk/pdbsum/3amp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3amp ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q60032_THEMT Q60032_THEMT] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Cellulases have been used in many applications to treat various carbohydrate-containing materials. Thermotoga maritima cellulase 12A (TmCel12A) belongs to the GH12 family of glycoside hydrolases. It is a beta-1,4-endoglucanase that degrades cellulose molecules into smaller fragments, facilitating further utilization of the carbohydrate. Because of its hyperthermophilic nature, the enzyme is especially suitable for industrial applications. Here the crystal structure of TmCel12A was determined by using an active-site mutant E134C and its mercury-containing derivatives. It adopts a beta-jellyroll protein fold typical of the GH12-family enzymes, with two curved beta-sheets A and B and a central active-site cleft. Structural comparison with other GH12 enzymes shows significant differences, as found in two longer and highly twisted beta-strands B8 and B9 and several loops. A unique Loop A3-B3 that contains Arg60 and Tyr61 stabilizes the substrate by hydrogen bonding and stacking, as observed in the complex crystals with cellotetraose and cellobiose. The high-resolution structures allow clear elucidation of the network of interactions between the enzyme and its substrate. The sugar residues bound to the enzyme appear to be more ordered in the -2 and -1 subsites than in the +1, +2 and -3 subsites. In the E134C crystals the bound -1 sugar at the cleavage site consistently show the alpha-anomeric configuration, implicating an intermediate-like structure. Proteins 2011; (c) 2011 Wiley-Liss, Inc. | |||
Crystal structure and substrate-binding mode of cellulase 12A from Thermotoga maritima.,Cheng YS, Ko TP, Wu TH, Ma Y, Huang CH, Lai HL, Wang AH, Liu JR, Guo RT Proteins. 2011 Apr;79(4):1193-204. doi: 10.1002/prot.22953. Epub 2011 Jan, 25. PMID:21268113<ref>PMID:21268113</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3amp" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Glucanase 3D structures|Glucanase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Thermotoga maritima]] | |||
[[Category: Cheng Y-S]] | |||
[[Category: Guo R-T]] | |||
[[Category: Ko T-P]] | |||
[[Category: Liu J-R]] | |||
Latest revision as of 18:49, 4 October 2023
E134C-Cellotetraose complex of cellulase 12A from thermotoga maritimaE134C-Cellotetraose complex of cellulase 12A from thermotoga maritima
Structural highlights
FunctionPublication Abstract from PubMedCellulases have been used in many applications to treat various carbohydrate-containing materials. Thermotoga maritima cellulase 12A (TmCel12A) belongs to the GH12 family of glycoside hydrolases. It is a beta-1,4-endoglucanase that degrades cellulose molecules into smaller fragments, facilitating further utilization of the carbohydrate. Because of its hyperthermophilic nature, the enzyme is especially suitable for industrial applications. Here the crystal structure of TmCel12A was determined by using an active-site mutant E134C and its mercury-containing derivatives. It adopts a beta-jellyroll protein fold typical of the GH12-family enzymes, with two curved beta-sheets A and B and a central active-site cleft. Structural comparison with other GH12 enzymes shows significant differences, as found in two longer and highly twisted beta-strands B8 and B9 and several loops. A unique Loop A3-B3 that contains Arg60 and Tyr61 stabilizes the substrate by hydrogen bonding and stacking, as observed in the complex crystals with cellotetraose and cellobiose. The high-resolution structures allow clear elucidation of the network of interactions between the enzyme and its substrate. The sugar residues bound to the enzyme appear to be more ordered in the -2 and -1 subsites than in the +1, +2 and -3 subsites. In the E134C crystals the bound -1 sugar at the cleavage site consistently show the alpha-anomeric configuration, implicating an intermediate-like structure. Proteins 2011; (c) 2011 Wiley-Liss, Inc. Crystal structure and substrate-binding mode of cellulase 12A from Thermotoga maritima.,Cheng YS, Ko TP, Wu TH, Ma Y, Huang CH, Lai HL, Wang AH, Liu JR, Guo RT Proteins. 2011 Apr;79(4):1193-204. doi: 10.1002/prot.22953. Epub 2011 Jan, 25. PMID:21268113[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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