1c9j: Difference between revisions

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[[Image:1c9j.jpg|left|200px]]


{{Structure
==BACILLUS LENTUS SUBTILISIN K27R/N87S/V104Y/N123S/T274A VARIANT==
|PDB= 1c9j |SIZE=350|CAPTION= <scene name='initialview01'>1c9j</scene>, resolution 1.8&Aring;
<StructureSection load='1c9j' size='340' side='right'caption='[[1c9j]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
<table><tr><td colspan='2'>[[1c9j]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lederbergia_lenta Lederbergia lenta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C9J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C9J FirstGlance]. <br>
|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]  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
}}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1c9j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c9j OCA], [https://pdbe.org/1c9j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c9j RCSB], [https://www.ebi.ac.uk/pdbsum/1c9j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c9j ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SUBS_LEDLE SUBS_LEDLE] Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c9/1c9j_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1c9j ConSurf].
<div style="clear:both"></div>


'''BACILLUS LENTUS SUBTILISIN K27R/N87S/V104Y/N123S/T274A VARIANT'''
==See Also==
 
*[[Subtilisin 3D structures|Subtilisin 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
The three-dimensional structures of engineered variants of Bacillus lentus subtilisin having increased enzymatic activity, K27R/N87S/V104Y/N123S/T274A (RSYSA) and N76D/N87S/S103A/V104I (DSAI), were determined by X-ray crystallography. In addition to identifying changes in atomic position we report a method that identifies protein segments having altered flexibility. The method utilizes a statistical analysis of variance to delineate main-chain temperature factors that represent significant departures from the overall variance between equivalent regions seen throughout the structure. This method reveals changes in main-chain mobility in both variants. Residues 125-127 have increased mobility in the RSYSA variant while residues 100-104 have decreased mobility in the DSAI variant. These segments are located at the substrate-binding site and changes in their mobility are believed to relate to the observed changes in proteolytic activity. The effect of altered crystal lattice contacts on segment flexibility becomes apparent when identical variants, determined in two crystal forms, are compared with the native enzyme.
[[Category: Large Structures]]
 
[[Category: Lederbergia lenta]]
==About this Structure==
[[Category: Bott R]]
1C9J is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_lentus Bacillus lentus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C9J OCA].
 
==Reference==
Engineered Bacillus lentus subtilisins having altered flexibility., Graycar T, Knapp M, Ganshaw G, Dauberman J, Bott R, J Mol Biol. 1999 Sep 10;292(1):97-109. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10493860 10493860]
[[Category: Bacillus lentus]]
[[Category: Single protein]]
[[Category: Subtilisin]]
[[Category: Bott, R.]]
[[Category: CA]]
[[Category: SO4]]
[[Category: altered flexibility]]
[[Category: hydrolase]]
[[Category: subtilisin]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:21:35 2008''

Latest revision as of 09:41, 7 February 2024

BACILLUS LENTUS SUBTILISIN K27R/N87S/V104Y/N123S/T274A VARIANTBACILLUS LENTUS SUBTILISIN K27R/N87S/V104Y/N123S/T274A VARIANT

Structural highlights

1c9j is a 1 chain structure with sequence from Lederbergia lenta. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SUBS_LEDLE Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1c9j, resolution 1.80Å

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