1wve: Difference between revisions

Latest revision as of 07:42, 23 October 2024

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

Structural highlights

1wve is a 4 chain structure with sequence from Pseudomonas putida. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.85Å
Ligands:	ACY, CL, FAD, HEM, TRS
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DH4C_PSEPU

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Cunane LM, Chen ZW, McIntire WS, Mathews FS. p-Cresol methylhydroxylase: alteration of the structure of the flavoprotein subunit upon its binding to the cytochrome subunit. Biochemistry. 2005 Mar 1;44(8):2963-73. PMID:15723539 doi:10.1021/bi048020r

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Cunane LM, Chen ZW, McIntire WS, Mathews FS. p-Cresol methylhydroxylase: alteration of the structure of the flavoprotein subunit upon its binding to the cytochrome subunit. Biochemistry. 2005 Mar 1;44(8):2963-73. PMID:15723539 doi:10.1021/bi048020r

[1]

@@ Line 1: / Line 1: @@
 ==p-Cresol Methylhydroxylase: Alteration of the Structure of the Flavoprotein Subunit upon its Binding to the Cytochrome Subunit==
-<StructureSection load='1wve' size='340' side='right' caption='[[1wve]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
+<StructureSection load='1wve' size='340' side='right'caption='[[1wve]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1wve]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_fluorescens_putidus"_flugge_1886 "bacillus fluorescens putidus" flugge 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WVE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WVE FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1wve]] is a 4 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=1WVE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WVE FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1dii|1dii]], [[1diq|1diq]], [[1wvf|1wvf]]</td></tr>
+<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=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/4-methylphenol_dehydrogenase_(hydroxylating) 4-methylphenol dehydrogenase (hydroxylating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.17.99.1 1.17.99.1] </span></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=1wve FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wve OCA], [https://pdbe.org/1wve PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wve RCSB], [https://www.ebi.ac.uk/pdbsum/1wve PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wve ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wve FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wve OCA], [http://pdbe.org/1wve PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1wve RCSB], [http://www.ebi.ac.uk/pdbsum/1wve PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1wve ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CY4C_PSEPU CY4C_PSEPU]] This is the heme-containing component of the p-cresol methylhydroxylase. It accepts electrons from the flavoprotein subunit.
+[https://www.uniprot.org/uniprot/DH4C_PSEPU DH4C_PSEPU]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 16: / Line 15: @@
    <jmolCheckbox>
      <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wv/1wve_consurf.spt"</scriptWhenChecked>
-     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
      <text>to colour the structure by Evolutionary Conservation</text>
    </jmolCheckbox>
@@ Line 32: / Line 31: @@
 ==See Also==
-*[[Flavocytochrome|Flavocytochrome]]
+*[[Flavocytochrome 3D structures|Flavocytochrome 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Bacillus fluorescens putidus flugge 1886]]
+[[Category: Large Structures]]
-[[Category: Chen, Z W]]
+[[Category: Pseudomonas putida]]
-[[Category: Cunane, L M]]
+[[Category: Chen Z-W]]
-[[Category: Mathews, F S]]
+[[Category: Cunane LM]]
-[[Category: McIntire, W S]]
+[[Category: Mathews FS]]
-[[Category: Electron-transfer]]
+[[Category: McIntire WS]]
-[[Category: Fad]]
-[[Category: Flavocytochrome]]
-[[Category: Heme]]
-[[Category: Oxidoreductase]]

1wve: Difference between revisions

Latest revision as of 07:42, 23 October 2024

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

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