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==The structure of Acidothermus cellulolyticus family 74 glycoside hydrolase==
==The structure of Acidothermus cellulolyticus family 74 glycoside hydrolase==
<StructureSection load='4lgn' size='340' side='right' caption='[[4lgn]], [[Resolution|resolution]] 1.82&Aring;' scene=''>
<StructureSection load='4lgn' size='340' side='right'caption='[[4lgn]], [[Resolution|resolution]] 1.82&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4lgn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Acic1 Acic1]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LGN FirstGlance]. <br>
<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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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>
</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Acel_0618 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=351607 ACIC1])</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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4lgn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lgn OCA], [http://pdbe.org/4lgn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4lgn RCSB], [http://www.ebi.ac.uk/pdbsum/4lgn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4lgn ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0LSI1_ACIC1 A0LSI1_ACIC1]
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Acic1]]
[[Category: Acidothermus cellulolyticus 11B]]
[[Category: Alahuhta, P M]]
[[Category: Large Structures]]
[[Category: Lunin, V V]]
[[Category: Alahuhta PM]]
[[Category: Cellulose binding protein]]
[[Category: Lunin VV]]
[[Category: Gh74]]
[[Category: Xyloglucanase]]

Revision as of 13:59, 14 December 2022

The structure of Acidothermus cellulolyticus family 74 glycoside hydrolaseThe structure of Acidothermus cellulolyticus family 74 glycoside hydrolase

Structural highlights

4lgn is a 1 chain structure with sequence from Acidothermus cellulolyticus 11B. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

A0LSI1_ACIC1

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. ↑ Alahuhta M, Adney WS, Himmel ME, Lunin VV. Structure of Acidothermus cellulolyticus family 74 glycoside hydrolase at 1.82 A resolution. 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 doi:http://dx.doi.org/10.1107/S1744309113030005

4lgn, resolution 1.82Å

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