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==P450cin Active Site Water: Implications for Substrate Binding and Solvent Accessibility==
==P450cin Active Site Water: Implications for Substrate Binding and Solvent Accessibility==
<StructureSection load='4l77' size='340' side='right' caption='[[4l77]], [[Resolution|resolution]] 1.38&Aring;' scene=''>
<StructureSection load='4l77' size='340' side='right'caption='[[4l77]], [[Resolution|resolution]] 1.38&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4l77]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Citrobacter_braakii Citrobacter braakii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L77 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4L77 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4l77]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Citrobacter_braakii Citrobacter braakii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L77 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4L77 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CNL:1,3,3-TRIMETHYL-2-OXABICYCLO[2.2.2]OCTANE'>CNL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.379&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4l6g|4l6g]], [[4lht|4lht]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CNL:1,3,3-TRIMETHYL-2-OXABICYCLO[2.2.2]OCTANE'>CNL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CIN A, cinA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=57706 Citrobacter braakii])</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=4l77 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l77 OCA], [https://pdbe.org/4l77 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4l77 RCSB], [https://www.ebi.ac.uk/pdbsum/4l77 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4l77 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=4l77 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l77 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4l77 RCSB], [http://www.ebi.ac.uk/pdbsum/4l77 PDBsum]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/CINA_CITBR CINA_CITBR]] Involved in the degradation of cineol (eucalyptol). Catalyzes the initial hydroxylation of cineole exclusively at the pro-R carbon to give the (S)-6beta-hydroxycineole. Cineole is the natural substrate of CinA.  
[https://www.uniprot.org/uniprot/CINA_CITBR CINA_CITBR] Involved in the degradation of cineol (eucalyptol). Catalyzes the initial hydroxylation of cineole exclusively at the pro-R carbon to give the (S)-6beta-hydroxycineole. Cineole is the natural substrate of CinA.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
In P450cin, Tyr81, Asp241, Asn242, two water molecules, and the substrate participate in a complex H-bonded network. The role of this H-bonded network in substrate binding and catalysis has been probed by crystallography, spectroscopy, kinetics, isothermal titration calorimetry (ITC), and molecular dynamics. For the Y81F mutant, the substrate binds about 20-fold more weakly and Vmax decreases by about 30% in comparison to WT. The enhanced susceptibility of the heme to H2O2-mediated destruction in Y81F suggests that this mutant favors the open, low-spin conformational state. Asn242 H-bonds directly with the substrate, and replacing this residue with Ala results in water taking the place of the missing Asn side chain. This mutant exhibits a 70% decrease in activity. Crystal structures and molecular dynamics simulations of substrate-bound complexes show that the solvent has more ready access to the active site, especially for the N242A mutant. This accounts for about a 64% uncoupling of electron transfer from substrate hydroxylation. These data indicate the importance of the interconnected water network on substrate binding and on the open/closed conformational equilibrium, which are both critically important for maintaining high-coupling efficiency.
 
P450cin Active Site Water: Implications for Substrate Binding and Solvent Accessibility.,Madrona Y, Hollingsworth SA, Khan B, Poulos TL Biochemistry. 2013 Jul 18. PMID:23829586<ref>PMID:23829586</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
==See Also==
</div>
*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Citrobacter braakii]]
[[Category: Citrobacter braakii]]
[[Category: Madrona, Y]]
[[Category: Large Structures]]
[[Category: Poulos, T L]]
[[Category: Madrona Y]]
[[Category: Cindoxin]]
[[Category: Poulos TL]]
[[Category: Heme]]
[[Category: Monooxygenase]]
[[Category: Oxidoreductase]]
[[Category: P450]]

Latest revision as of 15:17, 1 March 2024

P450cin Active Site Water: Implications for Substrate Binding and Solvent AccessibilityP450cin Active Site Water: Implications for Substrate Binding and Solvent Accessibility

Structural highlights

4l77 is a 2 chain structure with sequence from Citrobacter braakii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.379Å
Ligands:, , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CINA_CITBR Involved in the degradation of cineol (eucalyptol). Catalyzes the initial hydroxylation of cineole exclusively at the pro-R carbon to give the (S)-6beta-hydroxycineole. Cineole is the natural substrate of CinA.

See Also

4l77, resolution 1.38Å

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