1qpu: Difference between revisions

Revision as of 19:58, 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:1qpu.png

Template:STRUCTURE 1qpu

SOLUTION STRUCTURE OF OXIDIZED ESCHERICHIA COLI CYTOCHROME B562SOLUTION STRUCTURE OF OXIDIZED ESCHERICHIA COLI CYTOCHROME B562

Template:ABSTRACT PUBMED 10393541

About this StructureAbout this Structure

1QPU is a Single protein structure of sequence from Escherichia coli. Full experimental information is available from OCA.

ReferenceReference

The solution structure of oxidized Escherichia coli cytochrome b562., Arnesano F, Banci L, Bertini I, Faraone-Mennella J, Rosato A, Barker PD, Fersht AR, Biochemistry. 1999 Jul 6;38(27):8657-70. PMID:10393541

Page seeded by OCA on Mon Jul 28 19:58:00 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1qpu.jpg|left|200px]]
+{{Seed}}
+[[Image:1qpu.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1qpu|  PDB=1qpu  |  SCENE=  }}
-'''SOLUTION STRUCTURE OF OXIDIZED ESCHERICHIA COLI CYTOCHROME B562'''
+===SOLUTION STRUCTURE OF OXIDIZED ESCHERICHIA COLI CYTOCHROME B562===
-==Overview==
+<!--
-The solution structure of the oxidized, paramagnetic form of cytochrome b562 from Escherichia coli (106 amino acids) is here reported as obtained from 1653 meaningful NOEs (from a total of 2051 unique NOEs), 33 (3)JHNHalpha values, and 339 pseudocontact shifts. The structure displays the typical four-helix bundle motif, and a disordered loop between helices alpha2 and alpha3, as found in the solid state. The solution structure has a conformation intermediate between the two independent solid-state molecules, although different orientations are observed for a few residues. The magnetic susceptibility tensor is similar to that of cytochrome c, which has the same ligands, although the anisotropy is somewhat smaller. This difference in the electronic structure is consistent with the thermal accessibility in cytochrome b562 of states with S &gt; 1/2. The structure is also compared with the solution structure of the apoprotein, and some information on the role of the cofactor on the protein folding and mobility is obtained. Helix alpha4 seems to be the most sensitive to the chemical environment in terms of structure and mobility. The pKa values affecting the hyperfine-shifted signals are also discussed. Quite intriguing is the comparison of the structure of cytochrome b562 with the available structures of cytochromes c' which display a similar folding motif and similar pKa values but very little sequence similarity.
+The line below this paragraph, {{ABSTRACT_PUBMED_10393541}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10393541 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10393541}}
 ==About this Structure==
-QPU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QPU OCA].
+QPU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QPU OCA].
 ==Reference==
@@ Line 31: / Line 35: @@
 [[Category: Four helix bundle]]
 [[Category: Hemoprotein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 06:33:59 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:58:00 2008''