View source for 2lqd


==Reduced and CO-bound cytochrome P450cam (CYP101A1)==
<StructureSection load='2lqd' size='340' side='right'caption='[[2lqd]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2lqd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LQD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LQD FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR,  models</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></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=2lqd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lqd OCA], [https://pdbe.org/2lqd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lqd RCSB], [https://www.ebi.ac.uk/pdbsum/2lqd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lqd ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CPXA_PSEPU CPXA_PSEPU] Involved in a camphor oxidation system.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Removal of substrate (+)-camphor from the active site of cytochrome P450(cam) (CYP101A1) results in nuclear magnetic resonance-detected perturbations in multiple regions of the enzyme. The (1)H-(15)N correlation map of substrate-free diamagnetic Fe(II) CO-bound CYP101A permits these perturbations to be mapped onto the solution structure of the enzyme. Residual dipolar couplings (RDCs) were measured for (15)N-(1)H amide pairs in two independent alignment media for the substrate-free enzyme and used as restraints in solvated molecular dynamics (MD) simulations to generate an ensemble of best-fit structures of the substrate-free enzyme in solution. Nuclear magnetic resonance-detected chemical shift perturbations reflect changes in the electronic environment of the NH pairs, such as hydrogen bonding and ring current shifts, and are observed for residues in the active site as well as in hinge regions between secondary structural features. RDCs provide information about relative orientations of secondary structures, and RDC-restrained MD simulations indicate that portions of a beta-rich region adjacent to the active site shift so as to partially occupy the vacancy left by removal of the substrate. The accessible volume of the active site is reduced in the substrate-free enzyme relative to the substrate-bound structure calculated using the same methods. Both symmetric and asymmetric broadening of multiple resonances observed upon substrate removal as well as localized increased errors in RDC fits suggest that an ensemble of enzyme conformations are present in the substrate-free form.

Solution Structural Ensembles of Substrate-Free Cytochrome P450(cam).,Asciutto EK, Young MJ, Madura J, Pochapsky SS, Pochapsky TC Biochemistry. 2012 Apr 10. PMID:22468842<ref>PMID:22468842</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2lqd" style="background-color:#fffaf0;"></div>

==See Also==
*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas putida]]
[[Category: Asciutto E]]
[[Category: Madura J]]
[[Category: Pochapsky SS]]
[[Category: Pochapsky TC]]
[[Category: Young MJ]]