From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1mpt.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1mpt.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1mpt| PDB=1mpt | SCENE= }} | | {{STRUCTURE_1mpt| PDB=1mpt | SCENE= }} |
| | | | |
| - | '''CRYSTAL STRUCTURE OF A NEW ALKALINE SERINE PROTEASE (M-PROTEASE) FROM BACILLUS SP. KSM-K16'''
| + | ===CRYSTAL STRUCTURE OF A NEW ALKALINE SERINE PROTEASE (M-PROTEASE) FROM BACILLUS SP. KSM-K16=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15299321}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15299321 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_15299321}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 32: |
Line 36: |
| | [[Category: Yamashita, O.]] | | [[Category: Yamashita, O.]] |
| | [[Category: Serine proteinase]] | | [[Category: Serine proteinase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:34:12 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 00:44:56 2008'' |
Revision as of 21:45, 2 July 2008
Template:STRUCTURE 1mpt
CRYSTAL STRUCTURE OF A NEW ALKALINE SERINE PROTEASE (M-PROTEASE) FROM BACILLUS SP. KSM-K16
Template:ABSTRACT PUBMED 15299321
About this Structure
1MPT is a Single protein structure of sequence from Bacillus clausii. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Jul 3 00:44:56 2008
