3vnd | pdb_00003vnd

Crystal structure of tryptophan synthase alpha-subunit from the psychrophile Shewanella frigidimarina K14-2

spinqualitylabelsall models 3vnd, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3vnd is a 8 chain structure with sequence from Acam 591. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: PE8, SO4 Related: 1v7y Gene: trpA (ACAM 591) Activity: Tryptophan synthase, with EC number 4.2.1.20 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [H1AFK5_SHEFR] The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.[HAMAP-Rule:MF_00131][SAAS:SAAS00108583] Publication Abstract from PubMed To investigate the molecular basis of cold adaptation of enzymes, we determined the crystal structure of the tryptophan synthase alpha subunit (SfTSA) from the psychrophile Shewanella frigidimarina K14-2 by X-ray analysis at 2.6-A resolution and also examined its physicochemical properties. SfTSA was found to have the following characteristics: (i) The stabilities against heat and denaturant of SfTSA were lower than those of an alpha subunit (EcTSA) from Escherichia coli. This lower equilibrium stability originated from both a faster unfolding rate and a slower refolding rate; (ii) the heat denaturation of SfTSA was completely reversible at pH 7.0 and the solubility of denatured SfTSA was higher than that of denatured EcTSA. The two-state transition of denaturation for SfTSA was highly cooperative, whereas the denaturation process of EcTSA was considerably more complex and (iii) the global structure of SfTSA was quite similar to those of alpha subunits from other species. Relative to those other proteins, SfTSA exhibited an increase in cavity volume and a decrease in the number of ion pairs. SfTSA also lacks a hydrogen bond near loop B, related to catalytic function. These characteristics of SfTSA might provide the conformational flexibility required for catalytic activity at low temperatures. Strategy for cold adaptation of the tryptophan synthase alpha subunit from the psychrophile Shewanella frigidimarina K14-2: crystal structure and physicochemical properties.,Mitsuya D, Tanaka S, Matsumura H, Urano N, Takano K, Ogasahara K, Takehira M, Yutani K, Ishida M J Biochem. 2014 Feb;155(2):73-82. doi: 10.1093/jb/mvt098. Epub 2013 Oct 25. PMID:24163283 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Tryptophan synthase 3D structures

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