1wve

From Proteopedia

(Difference between revisions)

Revision as of 16:28, 27 October 2021

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 "bacillus_fluorescens_putidus"_flugge_1886 "bacillus fluorescens putidus" flugge 1886. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , ,
Related:	1dii, 1diq, 1wvf
Activity:	4-methylphenol dehydrogenase (hydroxylating), with EC number 1.17.99.1
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CY4C_PSEPU] This is the heme-containing component of the p-cresol methylhydroxylase. It accepts electrons from the flavoprotein subunit.

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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1wve"

@@ Line 3: / Line 3: @@
 <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/"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 [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='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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1dii|1dii]], [[1diq|1diq]], [[1wvf|1wvf]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1dii|1dii]], [[1diq|1diq]], [[1wvf|1wvf]]</div></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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/4-methylphenol_dehydrogenase_(hydroxylating) 4-methylphenol dehydrogenase (hydroxylating)], with EC number [https://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'>[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>
+<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>
 </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/CY4C_PSEPU CY4C_PSEPU]] This is the heme-containing component of the p-cresol methylhydroxylase. It accepts electrons from the flavoprotein subunit.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1wve

From Proteopedia

Revision as of 16:28, 27 October 2021

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

Proteopedia Page Contributors and Editors (what is this?)

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