1n40: Difference between revisions

Revision as of 14:14, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1n40.png

Template:STRUCTURE 1n40

Atomic structure of CYP121, a mycobacterial P450Atomic structure of CYP121, a mycobacterial P450

Template:ABSTRACT PUBMED 12435731

About this StructureAbout this Structure

1N40 is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

ReferenceReference

Atomic structure of Mycobacterium tuberculosis CYP121 to 1.06 A reveals novel features of cytochrome P450., Leys D, Mowat CG, McLean KJ, Richmond A, Chapman SK, Walkinshaw MD, Munro AW, J Biol Chem. 2003 Feb 14;278(7):5141-7. Epub 2002 Nov 14. PMID:12435731

Page seeded by OCA on Mon Jul 28 14:14:15 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1n40.gif|left|200px]]
+{{Seed}}
+[[Image:1n40.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1n40|  PDB=1n40  |  SCENE=  }}
-'''Atomic structure of CYP121, a mycobacterial P450'''
+===Atomic structure of CYP121, a mycobacterial P450===
-==Overview==
+<!--
-The first structure of a P450 to an atomic resolution of 1.06 A has been solved for CYP121 from Mycobacterium tuberculosis. A comparison with P450 EryF (CYP107A1) reveals a remarkable overall similarity in fold with major differences residing in active site structural elements. The high resolution obtained allows visualization of several unusual aspects. The heme cofactor is bound in two distinct conformations while being notably kinked in one pyrrole group due to close interaction with the proline residue (Pro(346)) immediately following the heme iron-ligating cysteine (Cys(345)). The active site is remarkably rigid in comparison with the remainder of the structure, notwithstanding the large cavity volume of 1350 A(3). The region immediately surrounding the distal water ligand is remarkable in several aspects. Unlike other bacterial P450s, the I helix shows no deformation, similar to mammalian CYP2C5. In addition, the positively charged Arg(386) is located immediately above the heme plane, dominating the local structure. Putative proton relay pathways from protein surface to heme (converging at Ser(279)) are identified. Most interestingly, the electron density indicates weak binding of a dioxygen molecule to the P450. This structure provides a basis for rational design of putative antimycobacterial agents.
+The line below this paragraph, {{ABSTRACT_PUBMED_12435731}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12435731 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12435731}}
 ==About this Structure==
@@ Line 38: / Line 42: @@
 [[Category: Tb structural genomics consortium]]
 [[Category: Tbsgc]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 02:03:45 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 14:14:15 2008''