1MPT

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

Summary for 1MPT

• Entry DOI: 10.2210/pdb1mpt/pdb
• Descriptor: M-PROTEASE, CALCIUM ION (3 entities in total)
• Functional Keywords: serine proteinase
• Biological source: Bacillus clausii
• Total number of polymer chains: 1
• Total formula weight: 26823.59

Authors

Yamane, T.,Kani, T.,Hatanaka, T.,Suzuki, A.,Ashida, T.,Kobayashi, T.,Ito, S.,Yamashita, O. (deposition date: 1994-04-13, release date: 1994-06-22, Last modification date: 2024-02-14)

Primary citation

Yamane, T.,Kani, T.,Hatanaka, T.,Suzuki, A.,Ashida, T.,Kobatashi, T.,Ito, S.,Yamashita, O.
Structure of a new alkaline serine protease (M-protease) from Bacillus sp. KSM-K16.
Acta Crystallogr.,Sect.D, 51:199-206, 1995

PubMed Abstract: 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.

PubMed: 15299321
DOI: 10.1107/S0907444994009960

Experimental method

X-RAY DIFFRACTION (2.4 Å)