1ehb: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
Line 1: Line 1:
[[Image:1ehb.jpg|left|200px]]
{{Seed}}
[[Image:1ehb.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ehb|  PDB=1ehb  |  SCENE=  }}  
{{STRUCTURE_1ehb|  PDB=1ehb  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF RECOMBINANT TRYPSIN-SOLUBILIZED FRAGMENT OF CYTOCHROME B5'''
===CRYSTAL STRUCTURE OF RECOMBINANT TRYPSIN-SOLUBILIZED FRAGMENT OF CYTOCHROME B5===




==Overview==
<!--
The crystal structure of the recombinant trypsin-solubilized fragment of the microsomal cytochrome b(5) from bovine liver has been determined at 1.9 A resolution and compared with the reported crystal structure of the lipase-solubilized fragment of the membrane protein cytochrome b(5). The two structures are similar to each other. However, some detailed structural differences are observed: the conformation of the segment Asn16-Ser20 is quite different, some helices around the heme and some segments between the helices are shifted slightly, the heme is rotated about the normal of the mean plane of heme, one of the propionates of the heme exhibits a different conformation. The average coordination distances between the iron and the two nitrogen atoms of the imidazole ligands are the same in the two structures. Most of the structural differences can be attributed to the different intermolecular interactions which result from the crystal packing. The wild-type protein structure is also compared with its Val61His mutant, showing that the heme binding and the main chain conformations are basically identical with each other except for the local area of the mutation site. However, when Val61 is mutated to histidine, the large side chain of His61 is forced to point away from the heme pocket toward the solvent region, disturbing the micro-environment of the heme pocket and influencing the stability and the redox potential of the protein.
The line below this paragraph, {{ABSTRACT_PUBMED_10842340}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 10842340 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_10842340}}


==About this Structure==
==About this Structure==
Line 34: Line 38:
[[Category: Recombinant wild type]]
[[Category: Recombinant wild type]]
[[Category: Trypsin-cleaved fragment]]
[[Category: Trypsin-cleaved fragment]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:06:12 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:42:01 2008''

Revision as of 21:42, 30 June 2008

File:1ehb.png

Template:STRUCTURE 1ehb

CRYSTAL STRUCTURE OF RECOMBINANT TRYPSIN-SOLUBILIZED FRAGMENT OF CYTOCHROME B5

Template:ABSTRACT PUBMED 10842340

About this Structure

1EHB is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

Crystal structure of recombinant trypsin-solubilized fragment of cytochrome b(5) and the structural comparison with Val61His mutant., Wu J, Gan JH, Xia ZX, Wang YH, Wang WH, Xue LL, Xie Y, Huang ZX, Proteins. 2000 Aug 1;40(2):249-57. PMID:10842340

Page seeded by OCA on Tue Jul 1 00:42:01 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1ehb&oldid=592351"