This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1c9n

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (15:38, 13 March 2024) (edit) (undo)
 
(16 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1c9n.jpg|left|200px]]
 
-
{{Structure
+
==BACILLUS LENTUS SUBSTILISIN VARIANT (SER 87) K27R/V104Y/N123S/T274A==
-
|PDB= 1c9n |SIZE=350|CAPTION= <scene name='initialview01'>1c9n</scene>, resolution 1.5&Aring;
+
<StructureSection load='1c9n' size='340' side='right'caption='[[1c9n]], [[Resolution|resolution]] 1.50&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'>[[1c9n]] 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=1C9N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C9N 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]] 1.5&#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=SEB:O-BENZYLSULFONYL-SERINE'>SEB</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=1c9n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c9n OCA], [https://pdbe.org/1c9n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c9n RCSB], [https://www.ebi.ac.uk/pdbsum/1c9n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c9n 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/c9/1c9n_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=1c9n ConSurf].
 +
<div style="clear:both"></div>
-
'''BACILLUS LENTUS SUBSTILISIN VARIANT (SER 87) K27R/V104Y/N123S/T274A'''
+
==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]]
-
1C9N 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=1C9N 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: site-specific variant]]
+
-
[[Category: subtiliin]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:21:38 2008''
+

Current revision

BACILLUS LENTUS SUBSTILISIN VARIANT (SER 87) K27R/V104Y/N123S/T274A

PDB ID 1c9n

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1c9n"
Personal tools