2axx: Difference between revisions

Revision as of 19:13, 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:2axx.png

Template:STRUCTURE 2axx

THE SOLUTION STRUCTURE OF OXIDIZED RAT MICROSOMAL CYTOCHROME B5, NMR, 21 STRUCTURESTHE SOLUTION STRUCTURE OF OXIDIZED RAT MICROSOMAL CYTOCHROME B5, NMR, 21 STRUCTURES

Template:ABSTRACT PUBMED 9425037

About this StructureAbout this Structure

2AXX is a Single protein structure of sequence from Rattus norvegicus. Full experimental information is available from OCA.

ReferenceReference

The solution structure of oxidized rat microsomal cytochrome b5., Arnesano F, Banci L, Bertini I, Felli IC, Biochemistry. 1998 Jan 6;37(1):173-84. PMID:9425037

Page seeded by OCA on Mon Jul 28 19:13:27 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:2axx.gif|left|200px]]
+{{Seed}}
+[[Image:2axx.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2axx|  PDB=2axx  |  SCENE=  }}
-'''THE SOLUTION STRUCTURE OF OXIDIZED RAT MICROSOMAL CYTOCHROME B5, NMR, 21 STRUCTURES'''
+===THE SOLUTION STRUCTURE OF OXIDIZED RAT MICROSOMAL CYTOCHROME B5, NMR, 21 STRUCTURES===
-==Overview==
+<!--
-The solution structure of oxidized rat microsomal cytochrome b5 has been obtained from 1H NMR spectra measured at 800 MHz. The available assignment has been extended to 78% of the total protons and 95% of the residues. From 1372 meaningful NOEs, a family of 40 structures has been obtained through the program DYANA; 235 pseudocontact shifts have been then added as further constraints, obtaining an essentially similar family of structures. This latter family has been further refined through restrained energy minimization. The final RMSD values with respect to the average structure are 0.58 +/- 0.10 A and 1.05 +/- 0.11 A for backbone and heavy atoms, respectively. The high quality of the structure allows meaningful comparisons with the solution structure of the reduced protein, with the X-ray and solution structures of the oxidized bovine isoenzyme, and with the solution structure of the apoprotein. Upon loss of one electron, the heme plane undergoes a change in its orientation, possibly due to the change of the total charge. Propionate 7 appears to have a conformation which is dependent on the oxidation state of the iron. Helices alpha2 and alpha4 also experience changes in their average positions in the two oxidation states. Finally, the backbone NHs experience different exchange properties in the two oxidation states. While those present in the beta sheets forming the basis of the heme pocket are nonexchanging in both oxidation states, the NHs in the helices forming the heme-binding pocket are exchanging with the bulk solvent in the oxidized form, indicating larger local mobility in this state. This observation could suggest that, to optimize the electron transfer process, the local mobility should be properly tuned.
+The line below this paragraph, {{ABSTRACT_PUBMED_9425037}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9425037 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9425037}}
 ==About this Structure==
-AXX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AXX OCA].
+AXX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AXX OCA].
 ==Reference==
@@ Line 32: / Line 36: @@
 [[Category: Protein recognition]]
 [[Category: Solution structure]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 19:36:37 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:13:27 2008''