PDBsum entry 1mpt

Serine proteinase

PDB id: 1mpt

Contents

Protein chain

269 a.a. *

Metals

_CA ×2

Waters ×44

* Residue conservation analysis

PDB id:

1mpt

Name:

Serine proteinase

Title:

Crystal structure of a new alkaline serine protease (m-protease) from bacillus sp. Ksm-k16

Structure:

M-protease. Chain: a. Engineered: yes

Source:

Bacillus clausii. Organism_taxid: 66692. Strain: ksm-k16

Resolution:

2.40Å R-factor: 0.189

Authors:

T.Yamane,T.Kani,T.Hatanaka,A.Suzuki,T.Ashida,T.Kobayashi,S.Ito, O.Yamashita

Key ref:

T.Yamane et al. (1995). Structure of a new alkaline serine protease (M-protease) from Bacillus sp. KSM-K16. Acta Crystallogr D Biol Crystallogr, 51, 199-206. PubMed id: 15299321 DOI: 10.1107/S0907444994009960

Date:

13-Apr-94 Release date: 22-Jun-94

Protein chain

Q99405  (PRTM_BACSK) -  M-protease from Shouchella clausii (strain KSM-K16)

Seq: 380 a.a.

Struc: 269 a.a.

Enzyme reactions

• Enzyme class: E.C.3.4.21.- - ?????

DOI no: 10.1107/S0907444994009960

Acta Crystallogr D Biol Crystallogr 51:199-206 (1995)

PubMed id: 15299321

Structure of a new alkaline serine protease (M-protease) from Bacillus sp. KSM-K16.

T.Yamane, T.Kani, T.Hatanaka, A.Suzuki, T.Ashida, T.Kobatashi, S.Ito, O.Yamashita.

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.

Selected figure(s)

Figure 2.
Fig. 2. Luzzati plots of R factor versus resolution (l/2d). All reflections in the resolution range 7.0-2.4 A with Fo > 3tr(F) are used.

Figure 10.
Fig. 10. Stereoviews of the active site in M-protease. (a) The 2Fo -Fc electron density contoured at 1.4a level is superposed. (b) The struc- ture in SBC (thin lines) and the Fo -Fc electron density contoured at 2o level are superposed.

The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (1995, 51, 199-206) copyright 1995.

Figures were selected by an automated process.