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< | ==Crystal structure of exo-1,3/1,4-beta-glucanase (EXOP) from Pseudoalteromonas sp. BB1== | ||
<StructureSection load='3ut0' size='340' side='right'caption='[[3ut0]], [[Resolution|resolution]] 2.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3ut0]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudoalteromonas_sp._BB1 Pseudoalteromonas sp. BB1]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3f93 3f93]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UT0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UT0 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]] 2.3Å</td></tr> | |||
-- | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=3ut0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ut0 OCA], [https://pdbe.org/3ut0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ut0 RCSB], [https://www.ebi.ac.uk/pdbsum/3ut0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ut0 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q0QJA3_9GAMM Q0QJA3_9GAMM] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Following the discovery of an exo-1,3/1,4-beta-glucanase (glycoside hydrolase family 3) from a seaweed-associated bacterium Pseudoalteromonas sp. BB1, the recombinant three-domain protein (ExoP) was crystallized and its structure solved to 2.3A resolution. The first two domains of ExoP, both of which contribute to the architecture of the active site, are similar to those of the two-domain barley homologue ExoI with a distinctive Trp-Trp clamp at the +1 subsite, although ExoI displays broader specificity towards beta-glycosidic linkages. Notably excision of the third domain of ExoP results in an inactive enzyme. Domain 3 has a beta-sandwich structure and was shown by circular dichroism to be more temperature stable than the native enzyme. It makes relatively few contacts to domain 1 and none at all to domain 2. Two of the domain 3 residues involved at the interface, Q683 (forming one hydrogen bond) and Q676 (forming two) were mutated to alanine. Variant Q676A retained about half the activity of native ExoP but the Q683A variant was severely attenuated. The crystal structure of Q683A-ExoP indicated that domain 3 was highly mobile and that Q683 is critical to the stabilization of ExoP by domain 3. SAXS data lent support to this proposal. Domain 3 does not appear to be an obvious carbohydrate binding domain and is related neither in sequence nor structure to the additional domains characterized in other GH3 subgroups. Its major role appears to be for protein stability but it may also help orient substrate. | |||
Structure and activity of exo-1,3/1,4-beta-glucanase from marine bacterium Pseudoalteromonas sp. BB1 showing a novel C-terminal domain.,Nakatani Y, Cutfield SM, Cowieson NP, Cutfield JF FEBS J. 2011 Nov 29. doi: 10.1111/j.1742-4658.2011.08439.x. PMID:22129429<ref>PMID:22129429</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3ut0" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Beta-glucosidase 3D structures|Beta-glucosidase 3D structures]] | |||
*[[Glucanase 3D structures|Glucanase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
== | </StructureSection> | ||
[[ | [[Category: Large Structures]] | ||
[[Category: Pseudoalteromonas sp. BB1]] | |||
== | [[Category: Cutfield JF]] | ||
< | [[Category: Cutfield SM]] | ||
[[Category: | [[Category: Nakatani Y]] | ||
[[Category: | |||
[[Category: Cutfield | |||
[[Category: | |||
[[Category: | |||
Latest revision as of 15:14, 8 November 2023
Crystal structure of exo-1,3/1,4-beta-glucanase (EXOP) from Pseudoalteromonas sp. BB1Crystal structure of exo-1,3/1,4-beta-glucanase (EXOP) from Pseudoalteromonas sp. BB1
Structural highlights
FunctionPublication Abstract from PubMedFollowing the discovery of an exo-1,3/1,4-beta-glucanase (glycoside hydrolase family 3) from a seaweed-associated bacterium Pseudoalteromonas sp. BB1, the recombinant three-domain protein (ExoP) was crystallized and its structure solved to 2.3A resolution. The first two domains of ExoP, both of which contribute to the architecture of the active site, are similar to those of the two-domain barley homologue ExoI with a distinctive Trp-Trp clamp at the +1 subsite, although ExoI displays broader specificity towards beta-glycosidic linkages. Notably excision of the third domain of ExoP results in an inactive enzyme. Domain 3 has a beta-sandwich structure and was shown by circular dichroism to be more temperature stable than the native enzyme. It makes relatively few contacts to domain 1 and none at all to domain 2. Two of the domain 3 residues involved at the interface, Q683 (forming one hydrogen bond) and Q676 (forming two) were mutated to alanine. Variant Q676A retained about half the activity of native ExoP but the Q683A variant was severely attenuated. The crystal structure of Q683A-ExoP indicated that domain 3 was highly mobile and that Q683 is critical to the stabilization of ExoP by domain 3. SAXS data lent support to this proposal. Domain 3 does not appear to be an obvious carbohydrate binding domain and is related neither in sequence nor structure to the additional domains characterized in other GH3 subgroups. Its major role appears to be for protein stability but it may also help orient substrate. Structure and activity of exo-1,3/1,4-beta-glucanase from marine bacterium Pseudoalteromonas sp. BB1 showing a novel C-terminal domain.,Nakatani Y, Cutfield SM, Cowieson NP, Cutfield JF FEBS J. 2011 Nov 29. doi: 10.1111/j.1742-4658.2011.08439.x. PMID:22129429[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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