3rrx

Crystal Structure of Q683A mutant of Exo-1,3/1,4-beta-glucanase (ExoP) from Pseudoalteromonas sp. BB1

spinqualitylabelsall models 3rrx, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3rrx is a 1 chain structure with sequence from Pseudoalteromonas sp. BB1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.9Å Ligands: CA, EDO, NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q0QJA3_9GAMM 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Glucanase 3D structures

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