1mpt | pdb_00001mpt

CRYSTAL STRUCTURE OF A NEW ALKALINE SERINE PROTEASE (M-PROTEASE) FROM BACILLUS SP. KSM-K16

spinqualitylabelsall models 1mpt, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1mpt is a 1 chain structure with sequence from Bacsk. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA Activity: Subtilisin, with EC number 3.4.21.62 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 An alkaline serine protease, M-protease, from Bacillus sp. KSM-K16 has been crystallized. Two morphologically different crystal forms were obtained. Crystal data of form 1: space group P2(1)2(1)2(1), a = 47.3, b = 62.5, c = 75.6 A, V = 2.23 x 10(5) A(3), Z = 4 and V(m) = 2.09 A(3) Da(-1). Crystal data of form 2: space group P2(1)2(1)2(1), a = 75.82 (2), b = 57.79 (2), c = 54.19 (1) A, V = 2.29 (2) x 10(5) A(3), Z = 4 and V(m) = 2.15 A(3) Da(-1). The crystal structure of M-protease in form 2 has been solved by molecular replacement using the atomic model of subtilisin Carlsberg (SBC) which is 60% homologous with M-protease, and refined to the crystallographic R-factor of 0.189 for 7004 reflections with F(o)/sigma(F) > 3 between 7 and 2.4 A resolution. The final model of M-protease contains 1882 protein atoms, two calcium ions and 44 water molecules. The three-dimensional structure of M-protease is essentially similar to other subtilisins of known structure. The 269 C(alpha) positions of M-protease have an r.m.s. difference of 1.06 A with the corresponding positions of SBC. The crystal data of form 2 are close to those of SBC, though the structure determination of form 2 made it clear that it is not isomorphous to the crystal structure of SBC. The deletions of amino acids occur at the residues 36' and 160'-163' compared with SBC (numerals with primes show the numbering for SBC). The deletion of the four residues (160'-163') may significantly affect the lack of isomorphism between M-protease and SBC. Structure of a new alkaline serine protease (M-protease) from Bacillus sp. KSM-K16.,Yamane T, Kani T, Hatanaka T, Suzuki A, Ashida T, Kobatashi T, Ito S, Yamashita O Acta Crystallogr D Biol Crystallogr. 1995 Mar 1;51(Pt 2):199-206. PMID:15299321 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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