1cpt: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
New page: left|200px<br /><applet load="1cpt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cpt, resolution 2.3Å" /> '''CRYSTAL STRUCTURE AND...
 
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
 
(18 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1cpt.jpg|left|200px]]<br /><applet load="1cpt" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1cpt, resolution 2.3&Aring;" />
'''CRYSTAL STRUCTURE AND REFINEMENT OF CYTOCHROME P450-TERP AT 2.3 ANGSTROMS RESOLUTION'''<br />


==Overview==
==CRYSTAL STRUCTURE AND REFINEMENT OF CYTOCHROME P450-TERP AT 2.3 ANGSTROMS RESOLUTION==
Cytochrome P450terp is a class I (mitochondrial/bacterial) P450 that, catalyzes the hydroxylation of alpha-terpineol as part of the catabolic, assimilation of this compound by a pseudomonad species. Crystals grown, from the purified protein have the symmetry of space group P6(1)22, and, cell dimensions a = b = 69.4 A, c = 456.6 A, alpha = beta = 90 degrees, gamma = 120 degrees. Diffraction data were collected at the Cornell High, Energy Synchrotron Source, and the structure of P450terp was solved by a, combination of molecular replacement and multiple isomorphous replacement, techniques. A model of P450terp was built and refined against native data, to an R-factor of 18.9% for data with I &gt; or = sigma(I) between 6.0 A and, 2.3 A resolution. This model contains 412 of the 428 P450terp amino acid, residues; the loop between helices F and G is disordered in the crystal., While the overall fold of P450terp is very similar to that of P450cam, only three-quarters of the C alpha positions can be superimposed, to a, root-mean-square deviation of only 1.87 A. The mode of substrate binding, by P450terp can be predicted, and probable substrate contact residues, identified. The heme environment and side-chain positions in the adjacent, I-helix suggest possible modes of proton delivery in the catalytic cycle, of the enzyme.
<StructureSection load='1cpt' size='340' side='right'caption='[[1cpt]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1cpt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_sp. Pseudomonas sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CPT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CPT FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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=1cpt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cpt OCA], [https://pdbe.org/1cpt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cpt RCSB], [https://www.ebi.ac.uk/pdbsum/1cpt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cpt ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CPXL_PSESP CPXL_PSESP] Catalyzes the hydroxylation of alpha-terpineol.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cp/1cpt_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1cpt ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cytochrome P450terp is a class I (mitochondrial/bacterial) P450 that catalyzes the hydroxylation of alpha-terpineol as part of the catabolic assimilation of this compound by a pseudomonad species. Crystals grown from the purified protein have the symmetry of space group P6(1)22, and cell dimensions a = b = 69.4 A, c = 456.6 A, alpha = beta = 90 degrees, gamma = 120 degrees. Diffraction data were collected at the Cornell High Energy Synchrotron Source, and the structure of P450terp was solved by a combination of molecular replacement and multiple isomorphous replacement techniques. A model of P450terp was built and refined against native data, to an R-factor of 18.9% for data with I &gt; or = sigma(I) between 6.0 A and 2.3 A resolution. This model contains 412 of the 428 P450terp amino acid residues; the loop between helices F and G is disordered in the crystal. While the overall fold of P450terp is very similar to that of P450cam, only three-quarters of the C alpha positions can be superimposed, to a root-mean-square deviation of only 1.87 A. The mode of substrate binding by P450terp can be predicted, and probable substrate contact residues identified. The heme environment and side-chain positions in the adjacent I-helix suggest possible modes of proton delivery in the catalytic cycle of the enzyme.


==About this Structure==
Crystal structure and refinement of cytochrome P450terp at 2.3 A resolution.,Hasemann CA, Ravichandran KG, Peterson JA, Deisenhofer J J Mol Biol. 1994 Mar 4;236(4):1169-85. PMID:8120894<ref>PMID:8120894</ref>
1CPT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_sp. Pseudomonas sp.] with HEM as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CPT OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Crystal structure and refinement of cytochrome P450terp at 2.3 A resolution., Hasemann CA, Ravichandran KG, Peterson JA, Deisenhofer J, J Mol Biol. 1994 Mar 4;236(4):1169-85. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8120894 8120894]
</div>
[[Category: Pseudomonas sp.]]
<div class="pdbe-citations 1cpt" style="background-color:#fffaf0;"></div>
[[Category: Single protein]]
[[Category: Deisenhofer, J.]]
[[Category: Hasemann, C.A.]]
[[Category: Peterson, J.A.]]
[[Category: Ravichandran, K.G.]]
[[Category: HEM]]
[[Category: oxidoreductase(oxygenase)]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:39:36 2007''
==See Also==
*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas sp]]
[[Category: Deisenhofer J]]
[[Category: Hasemann CA]]
[[Category: Peterson JA]]
[[Category: Ravichandran KG]]

Latest revision as of 05:37, 13 August 2026

CRYSTAL STRUCTURE AND REFINEMENT OF CYTOCHROME P450-TERP AT 2.3 ANGSTROMS RESOLUTION

1cpt, resolution 2.30Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1cpt&oldid=4475571"