This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


4l77

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (12:17, 1 March 2024) (edit) (undo)
 
(2 intermediate revisions not shown.)
Line 1: Line 1:
 +
==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]]
+

Current revision

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

PDB ID 4l77

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/4l77"
Personal tools