1bfu

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (11:01, 2 August 2023) (edit) (undo)
 
(15 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1bfu.jpg|left|200px]]
 
-
{{Structure
+
==SUBTILISIN CARLSBERG IN 20% DIOXANE==
-
|PDB= 1bfu |SIZE=350|CAPTION= <scene name='initialview01'>1bfu</scene>, resolution 2.2&Aring;
+
<StructureSection load='1bfu' size='340' side='right'caption='[[1bfu]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene>
+
<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>
-
|ACTIVITY= <span class='plainlinks'>[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] </span>
+
</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>
-
|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=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene></td></tr>
-
|DOMAIN=
+
<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>
-
|RELATEDENTRY=
+
</table>
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bfu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bfu OCA], [http://www.ebi.ac.uk/pdbsum/1bfu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bfu RCSB]</span>
+
== 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.
-
'''SUBTILISIN CARLSBERG IN 20% DIOXANE'''
+
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>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 1bfu" style="background-color:#fffaf0;"></div>
-
==Overview==
+
==See Also==
-
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.
+
*[[Subtilisin 3D structures|Subtilisin 3D structures]]
-
 
+
== References ==
-
==About this Structure==
+
<references/>
-
1BFU is a [[Single protein]] structure of sequence from [http://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].
+
__TOC__
-
 
+
</StructureSection>
-
==Reference==
+
-
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://www.ncbi.nlm.nih.gov/pubmed/9675126 9675126]
+
[[Category: Bacillus licheniformis]]
[[Category: Bacillus licheniformis]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Subtilisin]]
+
[[Category: Klibanov AM]]
-
[[Category: Klibanov, A M.]]
+
[[Category: Schmitke JL]]
-
[[Category: Schmitke, J L.]]
+
[[Category: Stern LJ]]
-
[[Category: Stern, L J.]]
+
-
[[Category: mixture]]
+
-
[[Category: organic solvent]]
+
-
[[Category: serine protease]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:00:03 2008''
+

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