4mdo: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4mdo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Humicola_grisea_var._thermoidea Humicola grisea var. thermoidea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MDO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MDO FirstGlance]. <br>
<table><tr><td colspan='2'>[[4mdo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Humicola_grisea_var._thermoidea Humicola grisea var. thermoidea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MDO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MDO FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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=4mdo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mdo OCA], [https://pdbe.org/4mdo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mdo RCSB], [https://www.ebi.ac.uk/pdbsum/4mdo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mdo ProSAT]</span></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=4mdo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mdo OCA], [https://pdbe.org/4mdo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mdo RCSB], [https://www.ebi.ac.uk/pdbsum/4mdo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mdo ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/O93784_HUMGT O93784_HUMGT]  
[https://www.uniprot.org/uniprot/O93784_HUMGT O93784_HUMGT]  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Product inhibition of beta-glucosidases (BGs) by glucose is considered to be a limiting step in enzymatic technologies for plant-biomass saccharification. Remarkably, some beta-glucosidases belonging to the GH1 family exhibit unusual properties, being tolerant to, or even stimulated by, high glucose concentrations. However, the structural basis for the glucose tolerance and stimulation of BGs is still elusive. To address this issue, the first crystal structure of a fungal beta-glucosidase stimulated by glucose was solved in native and glucose-complexed forms, revealing that the shape and electrostatic properties of the entrance to the active site, including the +2 subsite, determine glucose tolerance. The aromatic Trp168 and the aliphatic Leu173 are conserved in glucose-tolerant GH1 enzymes and contribute to relieving enzyme inhibition by imposing constraints at the +2 subsite that limit the access of glucose to the -1 subsite. The GH1 family beta-glucosidases are tenfold to 1000-fold more glucose tolerant than GH3 BGs, and comparative structural analysis shows a clear correlation between active-site accessibility and glucose tolerance. The active site of GH1 BGs is located in a deep and narrow cavity, which is in contrast to the shallow pocket in the GH3 family BGs. These findings shed light on the molecular basis for glucose tolerance and indicate that GH1 BGs are more suitable than GH3 BGs for biotechnological applications involving plant cell-wall saccharification.
Structural basis for glucose tolerance in GH1 beta-glucosidases.,de Giuseppe PO, Souza Tde A, Souza FH, Zanphorlin LM, Machado CB, Ward RJ, Jorge JA, Furriel Rdos P, Murakami MT Acta Crystallogr D Biol Crystallogr. 2014 Jun;70(Pt 6):1631-9. doi:, 10.1107/S1399004714006920. Epub 2014 May 24. PMID:24914974<ref>PMID:24914974</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4mdo" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Beta-glucosidase 3D structures|Beta-glucosidase 3D structures]]
*[[Beta-glucosidase 3D structures|Beta-glucosidase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Latest revision as of 15:26, 1 March 2024

Crystal structure of a GH1 beta-glucosidase from the fungus Humicola insolensCrystal structure of a GH1 beta-glucosidase from the fungus Humicola insolens

Structural highlights

4mdo is a 1 chain structure with sequence from Humicola grisea var. thermoidea. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.6Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

O93784_HUMGT

See Also

4mdo, resolution 2.60Å

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