2gv8

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:47, 30 August 2023) (edit) (undo)
 
(13 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2gv8.gif|left|200px]]
 
-
<!--
+
==Crystal structure of flavin-containing monooxygenase (FMO) from S.pombe and NADPH cofactor complex==
-
The line below this paragraph, containing "STRUCTURE_2gv8", creates the "Structure Box" on the page.
+
<StructureSection load='2gv8' size='340' side='right'caption='[[2gv8]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[2gv8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GV8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GV8 FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
-
-->
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene></td></tr>
-
{{STRUCTURE_2gv8| PDB=2gv8 | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2gv8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gv8 OCA], [https://pdbe.org/2gv8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gv8 RCSB], [https://www.ebi.ac.uk/pdbsum/2gv8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gv8 ProSAT], [https://www.topsan.org/Proteins/NYSGXRC/2gv8 TOPSAN]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/FMO1_SCHPO FMO1_SCHPO] Flavin-dependent oxidation of thiol-containing compounds. Probably required for the correct folding of disulfide-bonded proteins (By similarity).
 +
== 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/gv/2gv8_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=2gv8 ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Elimination of nonnutritional and insoluble compounds is a critical task for any living organism. Flavin-containing monooxygenases (FMOs) attach an oxygen atom to the insoluble nucleophilic compounds to increase solubility and thereby increase excretion. Here we analyze the functional mechanism of FMO from Schizosaccharomyces pombe using the crystal structures of the wild type and protein-cofactor and protein-substrate complexes. The structure of the wild-type FMO revealed that the prosthetic group FAD is an integral part of the protein. FMO needs NADPH as a cofactor in addition to the prosthetic group for its catalytic activity. Structures of the protein-cofactor and protein-substrate complexes provide insights into mechanism of action. We propose that FMOs exist in the cell as a complex with a reduced form of the prosthetic group and NADPH cofactor, readying them to act on substrates. The 4alpha-hydroperoxyflavin form of the prosthetic group represents a transient intermediate of the monooxygenation process. The oxygenated and reduced forms of the prosthetic group help stabilize interactions with cofactor and substrate alternately to permit continuous enzyme turnover.
-
'''Crystal structure of flavin-containing monooxygenase (FMO) from S.pombe and NADPH cofactor complex'''
+
Mechanism of action of a flavin-containing monooxygenase.,Eswaramoorthy S, Bonanno JB, Burley SK, Swaminathan S Proc Natl Acad Sci U S A. 2006 Jun 27;103(26):9832-7. Epub 2006 Jun 15. PMID:16777962<ref>PMID:16777962</ref>
-
 
+
-
 
+
-
==Overview==
+
-
Elimination of nonnutritional and insoluble compounds is a critical task for any living organism. Flavin-containing monooxygenases (FMOs) attach an oxygen atom to the insoluble nucleophilic compounds to increase solubility and thereby increase excretion. Here we analyze the functional mechanism of FMO from Schizosaccharomyces pombe using the crystal structures of the wild type and protein-cofactor and protein-substrate complexes. The structure of the wild-type FMO revealed that the prosthetic group FAD is an integral part of the protein. FMO needs NADPH as a cofactor in addition to the prosthetic group for its catalytic activity. Structures of the protein-cofactor and protein-substrate complexes provide insights into mechanism of action. We propose that FMOs exist in the cell as a complex with a reduced form of the prosthetic group and NADPH cofactor, readying them to act on substrates. The 4alpha-hydroperoxyflavin form of the prosthetic group represents a transient intermediate of the monooxygenation process. The oxygenated and reduced forms of the prosthetic group help stabilize interactions with cofactor and substrate alternately to permit continuous enzyme turnover.
+
-
==About this Structure==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
2GV8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GV8 OCA].
+
</div>
 +
<div class="pdbe-citations 2gv8" style="background-color:#fffaf0;"></div>
-
==Reference==
+
==See Also==
-
Mechanism of action of a flavin-containing monooxygenase., Eswaramoorthy S, Bonanno JB, Burley SK, Swaminathan S, Proc Natl Acad Sci U S A. 2006 Jun 27;103(26):9832-7. Epub 2006 Jun 15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16777962 16777962]
+
*[[Monooxygenase 3D structures|Monooxygenase 3D structures]]
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Large Structures]]
[[Category: Schizosaccharomyces pombe]]
[[Category: Schizosaccharomyces pombe]]
-
[[Category: Single protein]]
+
[[Category: Burley SK]]
-
[[Category: Burley, S K.]]
+
[[Category: Eswaramoorthy S]]
-
[[Category: Eswaramoorthy, S.]]
+
[[Category: Swaminathan S]]
-
[[Category: NYSGXRC, New York Structural GenomiX Research Consortium.]]
+
-
[[Category: Swaminathan, S.]]
+
-
[[Category: Cofactor complex]]
+
-
[[Category: Fad]]
+
-
[[Category: Fmo]]
+
-
[[Category: Nadph]]
+
-
[[Category: New york structural genomix research consortium]]
+
-
[[Category: Nysgxrc]]
+
-
[[Category: Oxygenase]]
+
-
[[Category: Protein structure initiative]]
+
-
[[Category: Psi]]
+
-
[[Category: Structural genomic]]
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:34:43 2008''
+

Current revision

Crystal structure of flavin-containing monooxygenase (FMO) from S.pombe and NADPH cofactor complex

PDB ID 2gv8

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/2gv8"
Personal tools