4lgn: Difference between revisions
New page: '''Unreleased structure''' The entry 4lgn is ON HOLD Authors: Alahuhta, P.M., Lunin, V.V. Description: The structure of Acidothermus cellulolyticus family 74 glycoside hydrolase |
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The | ==The structure of Acidothermus cellulolyticus family 74 glycoside hydrolase== | ||
<StructureSection load='4lgn' size='340' side='right'caption='[[4lgn]], [[Resolution|resolution]] 1.82Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4lgn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acidothermus_cellulolyticus_11B Acidothermus cellulolyticus 11B]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LGN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LGN 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]] 1.82Å</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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=4lgn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lgn OCA], [https://pdbe.org/4lgn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lgn RCSB], [https://www.ebi.ac.uk/pdbsum/4lgn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lgn ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0LSI1_ACIC1 A0LSI1_ACIC1] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Here, a 1.82 A resolution X-ray structure of a glycoside hydrolase family 74 (GH74) enzyme from Acidothermus cellulolyticus is reported. The resulting structure was refined to an R factor of 0.150 and an Rfree of 0.196. Structural analysis shows that five related structures have been reported with a secondary-structure similarity of between 75 and 89%. The five similar structures were all either Clostridium thermocellum or Geotrichum sp. M128 GH74 xyloglucanases. Structural analysis indicates that the A. cellulolyticus GH74 enzyme is an endoxyloglucanase, as it lacks a characteristic loop that blocks one end of the active site in exoxyloglucanases. Superimposition with the C. thermocellum GH74 shows that Asp451 and Asp38 are the catalytic residues. | |||
Structure of Acidothermus cellulolyticus family 74 glycoside hydrolase at 1.82 A resolution.,Alahuhta M, Adney WS, Himmel ME, Lunin VV Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Dec;69(Pt 12):1335-8. doi:, 10.1107/S1744309113030005. Epub 2013 Nov 28. PMID:24316824<ref>PMID:24316824</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4lgn" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Acidothermus cellulolyticus 11B]] | |||
[[Category: Large Structures]] | |||
[[Category: Alahuhta PM]] | |||
[[Category: Lunin VV]] |
Latest revision as of 19:19, 20 September 2023
The structure of Acidothermus cellulolyticus family 74 glycoside hydrolaseThe structure of Acidothermus cellulolyticus family 74 glycoside hydrolase
Structural highlights
FunctionPublication Abstract from PubMedHere, a 1.82 A resolution X-ray structure of a glycoside hydrolase family 74 (GH74) enzyme from Acidothermus cellulolyticus is reported. The resulting structure was refined to an R factor of 0.150 and an Rfree of 0.196. Structural analysis shows that five related structures have been reported with a secondary-structure similarity of between 75 and 89%. The five similar structures were all either Clostridium thermocellum or Geotrichum sp. M128 GH74 xyloglucanases. Structural analysis indicates that the A. cellulolyticus GH74 enzyme is an endoxyloglucanase, as it lacks a characteristic loop that blocks one end of the active site in exoxyloglucanases. Superimposition with the C. thermocellum GH74 shows that Asp451 and Asp38 are the catalytic residues. Structure of Acidothermus cellulolyticus family 74 glycoside hydrolase at 1.82 A resolution.,Alahuhta M, Adney WS, Himmel ME, Lunin VV Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Dec;69(Pt 12):1335-8. doi:, 10.1107/S1744309113030005. Epub 2013 Nov 28. PMID:24316824[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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