1bfu

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1bfu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bfu, resolution 2.2&Aring;" /> '''SUBTILISIN CARLSBERG ...)
Current revision (11:01, 2 August 2023) (edit) (undo)
 
(18 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1bfu.jpg|left|200px]]<br /><applet load="1bfu" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1bfu, resolution 2.2&Aring;" />
 
-
'''SUBTILISIN CARLSBERG IN 20% DIOXANE'''<br />
 
-
==Overview==
+
==SUBTILISIN CARLSBERG IN 20% DIOXANE==
-
The X-ray crystal structures of the protease subtilisin Carlsberg in 40%, acetonitrile and in 20% dioxane have been determined to at least 2.3 A, resolution, and their solvent binding patterns have been compared to those, observed in the neat organic solvents. The structures of the protein in, the two aqueous-organic mixtures are essentially the same as in pure, water, acetonitrile, and dioxane. Interestingly, the enzyme-bound organic, solvent molecules tend to congregate in the active site. Three of the five, bound acetonitrile molecules observed in the structure of subtilisin in, 40% acetonitrile are situated in the enzyme active site, as is the single, enzyme-bound dioxane molecule observed in 20% dioxane (whose location is, distinct from that of any bound acetonitrile molecule). Furthermore, the, organic solvent molecules detected in the enzyme active site in the, aqueous-organic mixtures are in the same locations as in the structures in, the corresponding neat organic solvents.
+
<StructureSection load='1bfu' size='340' side='right'caption='[[1bfu]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1bfu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BFU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BFU FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
 +
<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=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</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=1bfu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bfu OCA], [https://pdbe.org/1bfu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bfu RCSB], [https://www.ebi.ac.uk/pdbsum/1bfu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bfu ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/SUBC_BACLI SUBC_BACLI] Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides (Ref.4, PubMed:11109488). Shows high specificity for aromatic and hydrophobic amino acids in the P1 substrate position (PubMed:11109488). May play an important role in the degradation of feather keratin (PubMed:11109488).<ref>PMID:11109488</ref> <ref>PMID:4967581</ref>
 +
== 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/bf/1bfu_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=1bfu ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The X-ray crystal structures of the protease subtilisin Carlsberg in 40% acetonitrile and in 20% dioxane have been determined to at least 2.3 A resolution, and their solvent binding patterns have been compared to those observed in the neat organic solvents. The structures of the protein in the two aqueous-organic mixtures are essentially the same as in pure water, acetonitrile, and dioxane. Interestingly, the enzyme-bound organic solvent molecules tend to congregate in the active site. Three of the five bound acetonitrile molecules observed in the structure of subtilisin in 40% acetonitrile are situated in the enzyme active site, as is the single enzyme-bound dioxane molecule observed in 20% dioxane (whose location is distinct from that of any bound acetonitrile molecule). Furthermore, the organic solvent molecules detected in the enzyme active site in the aqueous-organic mixtures are in the same locations as in the structures in the corresponding neat organic solvents.
-
==About this Structure==
+
Organic solvent binding to crystalline subtilisin1 in mostly aqueous media and in the neat solvents.,Schmitke JL, Stern LJ, Klibanov AM Biochem Biophys Res Commun. 1998 Jul 20;248(2):273-7. PMID:9675126<ref>PMID:9675126</ref>
-
1BFU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis] with CA and DIO as [http://en.wikipedia.org/wiki/ligands ligands]. 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BFU OCA].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
Organic solvent binding to crystalline subtilisin1 in mostly aqueous media and in the neat solvents., Schmitke JL, Stern LJ, Klibanov AM, Biochem Biophys Res Commun. 1998 Jul 20;248(2):273-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9675126 9675126]
+
</div>
-
[[Category: Bacillus licheniformis]]
+
<div class="pdbe-citations 1bfu" style="background-color:#fffaf0;"></div>
-
[[Category: Single protein]]
+
-
[[Category: Subtilisin]]
+
-
[[Category: Klibanov, A.M.]]
+
-
[[Category: Schmitke, J.L.]]
+
-
[[Category: Stern, L.J.]]
+
-
[[Category: CA]]
+
-
[[Category: DIO]]
+
-
[[Category: mixtures]]
+
-
[[Category: organic solvent]]
+
-
[[Category: serine protease]]
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:37:05 2007''
+
==See Also==
 +
*[[Subtilisin 3D structures|Subtilisin 3D structures]]
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Bacillus licheniformis]]
 +
[[Category: Large Structures]]
 +
[[Category: Klibanov AM]]
 +
[[Category: Schmitke JL]]
 +
[[Category: Stern LJ]]

Current revision

SUBTILISIN CARLSBERG IN 20% DIOXANE

PDB ID 1bfu

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/1bfu"
Personal tools