1mpt

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[[Image:1mpt.gif|left|200px]]<br /><applet load="1mpt" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1mpt.gif|left|200px]]
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caption="1mpt, resolution 2.4&Aring;" />
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'''CRYSTAL STRUCTURE OF A NEW ALKALINE SERINE PROTEASE (M-PROTEASE) FROM BACILLUS SP. KSM-K16'''<br />
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{{Structure
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|PDB= 1mpt |SIZE=350|CAPTION= <scene name='initialview01'>1mpt</scene>, resolution 2.4&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Subtilisin Subtilisin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.62 3.4.21.62]
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|GENE=
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}}
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'''CRYSTAL STRUCTURE OF A NEW ALKALINE SERINE PROTEASE (M-PROTEASE) FROM BACILLUS SP. KSM-K16'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1MPT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_clausii Bacillus clausii] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Subtilisin Subtilisin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.62 3.4.21.62] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MPT OCA].
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1MPT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_clausii Bacillus clausii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MPT OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15299321 15299321]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15299321 15299321]
[[Category: Bacillus clausii]]
[[Category: Bacillus clausii]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: serine proteinase]]
[[Category: serine proteinase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:57:45 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:46:38 2008''

Revision as of 10:46, 20 March 2008

Image:1mpt.gif


PDB ID 1mpt

Drag the structure with the mouse to rotate
, resolution 2.4Å
Ligands:
Activity: Subtilisin, with EC number 3.4.21.62
Coordinates: save as pdb, mmCIF, xml



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.

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

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