1h71

Psychrophilic Protease from Pseudoalteromonas 'TAC II 18'

spinqualitylabelsall models 1h71, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1h71 is a 1 chain structure with sequence from Pseudomonas sp. tac ii 18. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, ZN Activity: Serralysin, with EC number 3.4.24.40 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Enzymes from psychrophilic organisms differ from their mesophilic counterparts in having a lower thermostability and a higher specific activity at low and moderate temperatures. It is in general accepted that psychrophilic enzymes are more flexible to allow easy accommodation and transformation of the substrates at low energy costs. Here, we report the structures of two crystal forms of the alkaline protease from an Antarctic Pseudomonas species (PAP), solved to 2.1- and 1.96-A resolution, respectively. Comparative studies of PAP structures with mesophilic counterparts show that the overall structures are similar but that the conformation of the substrate-free active site in PAP resembles that of the substrate-bound region of the mesophilic homolog, with both an active-site tyrosine and a substrate-binding loop displaying a conformation as in the substrate-bound form of the mesophilic proteases. Further, a region in the catalytic domain of PAP undergoes a conformational change with a loop movement as large as 13 A, induced by the binding of an extra calcium ion. Finally, the active site is more accessible due to deletions occurring in surrounding loop regions. Crystal structures of a psychrophilic metalloprotease reveal new insights into catalysis by cold-adapted proteases.,Aghajari N, Van Petegem F, Villeret V, Chessa JP, Gerday C, Haser R, Van Beeumen J Proteins. 2003 Mar 1;50(4):636-47. PMID:12577270 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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