4lgn
From Proteopedia
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- | {{STRUCTURE_4lgn| PDB=4lgn | SCENE= }} | ||
- | ===The structure of Acidothermus cellulolyticus family 74 glycoside hydrolase=== | ||
- | == | + | ==The structure of Acidothermus cellulolyticus family 74 glycoside hydrolase== |
- | [[4lgn]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LGN OCA]. | + | <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> |
- | [[Category: | + | </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> |
- | [[Category: | + | <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> |
- | [[Category: | + | <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]] |
Current revision
The structure of Acidothermus cellulolyticus family 74 glycoside hydrolase
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