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1mpt

From Proteopedia

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[[Image:1mpt.gif|left|200px]]
 
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{{Structure
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==CRYSTAL STRUCTURE OF A NEW ALKALINE SERINE PROTEASE (M-PROTEASE) FROM BACILLUS SP. KSM-K16==
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|PDB= 1mpt |SIZE=350|CAPTION= <scene name='initialview01'>1mpt</scene>, resolution 2.4&Aring;
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<StructureSection load='1mpt' size='340' side='right'caption='[[1mpt]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
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<table><tr><td colspan='2'>[[1mpt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Alkalihalobacillus_clausii_KSM-K16 Alkalihalobacillus clausii KSM-K16]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MPT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MPT FirstGlance]. <br>
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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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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mpt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mpt OCA], [https://pdbe.org/1mpt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mpt RCSB], [https://www.ebi.ac.uk/pdbsum/1mpt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mpt ProSAT]</span></td></tr>
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</table>
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'''CRYSTAL STRUCTURE OF A NEW ALKALINE SERINE PROTEASE (M-PROTEASE) FROM BACILLUS SP. KSM-K16'''
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== Function ==
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[https://www.uniprot.org/uniprot/PRTM_ALKCK PRTM_ALKCK] Alkaline serine protease that cleaves various substrates, including N-succinyl-Ala-Ala-Pro-Phe-pNA, N-succinyl-Ala-Ala-Pro-MetpNA, oxidized insulin B chain, casein, hemoglobin and scleroproteins, such as keratin, alpha-keratin and elastin.<ref>PMID:7632397</ref>
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== Evolutionary Conservation ==
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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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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) &gt; 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.
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Check<jmol>
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<jmolCheckbox>
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==About this Structure==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mp/1mpt_consurf.spt"</scriptWhenChecked>
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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].
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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==Reference==
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</jmolCheckbox>
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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]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1mpt ConSurf].
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[[Category: Bacillus clausii]]
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<div style="clear:both"></div>
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[[Category: Single protein]]
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== References ==
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[[Category: Subtilisin]]
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<references/>
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[[Category: Ashida, T.]]
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__TOC__
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[[Category: Hatanaka, T.]]
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</StructureSection>
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[[Category: Ito, S.]]
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[[Category: Alkalihalobacillus clausii KSM-K16]]
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[[Category: Kani, T.]]
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[[Category: Large Structures]]
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[[Category: Kobayashi, T.]]
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[[Category: Ashida T]]
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[[Category: Suzuki, A.]]
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[[Category: Hatanaka T]]
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[[Category: Yamane, T.]]
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[[Category: Ito S]]
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[[Category: Yamashita, O.]]
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[[Category: Kani T]]
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[[Category: CA]]
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[[Category: Kobayashi T]]
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[[Category: serine proteinase]]
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[[Category: Suzuki A]]
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[[Category: Yamane T]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:46:38 2008''
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[[Category: Yamashita O]]

Current revision

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

PDB ID 1mpt

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