View source for 3rrx


==Crystal Structure of Q683A mutant of Exo-1,3/1,4-beta-glucanase (ExoP) from Pseudoalteromonas sp. BB1==
<StructureSection load='3rrx' size='340' side='right'caption='[[3rrx]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3rrx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudoalteromonas_sp._BB1 Pseudoalteromonas sp. BB1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RRX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RRX 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]] 1.9&#8491;</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></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=3rrx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rrx OCA], [https://pdbe.org/3rrx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rrx RCSB], [https://www.ebi.ac.uk/pdbsum/3rrx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rrx 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 3rrx" style="background-color:#fffaf0;"></div>

==See Also==
*[[Glucanase 3D structures|Glucanase 3D structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudoalteromonas sp. BB1]]
[[Category: Cutfield JF]]
[[Category: Cutfield SM]]
[[Category: Nakatani Y]]