1wvf

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(New page: 200px<br /><applet load="1wvf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wvf, resolution 1.3&Aring;" /> '''p-Cresol Methylhydrox...)
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[[Image:1wvf.gif|left|200px]]<br /><applet load="1wvf" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1wvf, resolution 1.3&Aring;" />
 
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'''p-Cresol Methylhydroxylase: Alteration of the Structure of the Flavoprotein Subunit upon its Binding to the Cytochrome Subunit'''<br />
 
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==Overview==
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==p-Cresol Methylhydroxylase: Alteration of the Structure of the Flavoprotein Subunit upon its Binding to the Cytochrome Subunit==
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The structures of two forms of a recombinant flavoprotein have been, determined at high resolution and compared. These proteins are (1) the, flavocytochrome c p-cresol methylhydroxylase (rPCMH, 1.85 A resolution), and (2) the cytochrome-free flavoprotein subunit of rPCMH (PchF, 1.30 A, resolution). A significant conformational difference is observed in a, protein segment that is in contact with the re face of the isoalloxazine, ring of FAD when the structure of PchF is compared to the subunit in the, intact flavocytochrome. This structural change is important for optimum, catalytic function of the flavoprotein, which has been shown to be, dependent on the presence of the cytochrome subunit. This change results, in different protein-flavin and apparently different protein-substrate, interactions that have a "tuning effect" on the electronic and redox, properties of bound p-cresol and the covalently bound FAD. The, conformational change in the segment in the cofactor-binding site is, induced by a small rearrangement in the flavoprotein-cytochrome interface, region of the flavoprotein.
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<StructureSection load='1wvf' size='340' side='right'caption='[[1wvf]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1wvf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WVF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WVF FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.3&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1wvf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wvf OCA], [https://pdbe.org/1wvf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wvf RCSB], [https://www.ebi.ac.uk/pdbsum/1wvf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wvf ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DH4C_PSEPU DH4C_PSEPU]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The structures of two forms of a recombinant flavoprotein have been determined at high resolution and compared. These proteins are (1) the flavocytochrome c p-cresol methylhydroxylase (rPCMH, 1.85 A resolution) and (2) the cytochrome-free flavoprotein subunit of rPCMH (PchF, 1.30 A resolution). A significant conformational difference is observed in a protein segment that is in contact with the re face of the isoalloxazine ring of FAD when the structure of PchF is compared to the subunit in the intact flavocytochrome. This structural change is important for optimum catalytic function of the flavoprotein, which has been shown to be dependent on the presence of the cytochrome subunit. This change results in different protein-flavin and apparently different protein-substrate interactions that have a "tuning effect" on the electronic and redox properties of bound p-cresol and the covalently bound FAD. The conformational change in the segment in the cofactor-binding site is induced by a small rearrangement in the flavoprotein-cytochrome interface region of the flavoprotein.
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==About this Structure==
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p-Cresol methylhydroxylase: alteration of the structure of the flavoprotein subunit upon its binding to the cytochrome subunit.,Cunane LM, Chen ZW, McIntire WS, Mathews FS Biochemistry. 2005 Mar 1;44(8):2963-73. PMID:15723539<ref>PMID:15723539</ref>
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1WVF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida] with CL, FAD, ACY and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/4-cresol_dehydrogenase_(hydroxylating) 4-cresol dehydrogenase (hydroxylating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.17.99.1 1.17.99.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WVF OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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p-Cresol methylhydroxylase: alteration of the structure of the flavoprotein subunit upon its binding to the cytochrome subunit., Cunane LM, Chen ZW, McIntire WS, Mathews FS, Biochemistry. 2005 Mar 1;44(8):2963-73. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15723539 15723539]
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</div>
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[[Category: 4-cresol dehydrogenase (hydroxylating)]]
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<div class="pdbe-citations 1wvf" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Pseudomonas putida]]
[[Category: Pseudomonas putida]]
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[[Category: Single protein]]
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[[Category: Chen Z-W]]
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[[Category: Chen, Z.W.]]
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[[Category: Cunane LM]]
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[[Category: Cunane, L.M.]]
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[[Category: Mathews FS]]
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[[Category: Mathews, F.S.]]
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[[Category: McIntire WS]]
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[[Category: McIntire, W.S.]]
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[[Category: ACY]]
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[[Category: CL]]
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[[Category: FAD]]
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[[Category: GOL]]
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[[Category: electron-transfer]]
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[[Category: fad]]
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[[Category: flavoprotein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 05:42:02 2007''
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Current revision

p-Cresol Methylhydroxylase: Alteration of the Structure of the Flavoprotein Subunit upon its Binding to the Cytochrome Subunit

PDB ID 1wvf

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