This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1myi

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1myi.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1myi.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1myi| PDB=1myi | SCENE= }}
{{STRUCTURE_1myi| PDB=1myi | SCENE= }}
-
'''HIGH RESOLUTION X-RAY STRUCTURES OF PIG METMYOGLOBIN AND TWO CD3 MUTANTS MB(LYS45-> ARG) AND MB(LYS45-> SER)'''
+
===HIGH RESOLUTION X-RAY STRUCTURES OF PIG METMYOGLOBIN AND TWO CD3 MUTANTS MB(LYS45-> ARG) AND MB(LYS45-> SER)===
-
==Overview==
+
<!--
-
The structure of pig aquometmyoglobin has been refined to a crystallographic R-factor of 19.8% against X-ray diffraction data between 10- and 1.75-A spacing. The final structural model comprises two molecules of pig myoglobin, 233 water molecules, and two sulfate ions. A water molecule is coordinated to each of the heme iron atoms with an average Fe-OH2 bond distance of 2.19 A, and the mean Fe-N epsilon (proximal histidine-93) distance is 2.20 A. In contrast to the structure of sperm whale metmyoglobin, the iron is not significantly displaced from the plane of the heme. At the entrance to the heme pocket, the side-chain amino group of lysine-45 (CD3) is well-defined in the electron density map and forms salt-bridging interactions with the heme 6-propionate and with a sulfate ion. Serine and arginine replacements have been made previously at position 45 to examine the proposal that the CD3 side chain acts as a barrier to ligand entry into the protein. Crystal structures of the arginine-45 and serine-45 mutant metmyoglobins have been solved to 1.9 and 2.0 A resolution, respectively. In both cases the structural changes are confined to the site of mutation. Arginine-45 takes up a conformation closely similar to that observed for this residue in wild-type sperm whale myoglobin, in which it makes more extensive charge-charge and charge-dipole interactions and appears to restrict the movement of the distal histidine away from the ligand. The hydroxyl group of serine-45 is disordered, but it is clear that the effect of the mutation is to open up the solvent-exposed face of the heme pocket.
+
The line below this paragraph, {{ABSTRACT_PUBMED_1390659}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 1390659 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_1390659}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Wilson, K S.]]
[[Category: Wilson, K S.]]
[[Category: Oxygen storage]]
[[Category: Oxygen storage]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:52:14 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:01:56 2008''

Revision as of 10:02, 29 July 2008

Image:1myi.png

Template:STRUCTURE 1myi

HIGH RESOLUTION X-RAY STRUCTURES OF PIG METMYOGLOBIN AND TWO CD3 MUTANTS MB(LYS45-> ARG) AND MB(LYS45-> SER)

Template:ABSTRACT PUBMED 1390659

About this Structure

1MYI is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.

Reference

High-resolution X-ray structures of pig metmyoglobin and two CD3 mutants: Mb(Lys45----Arg) and Mb(Lys45----Ser)., Oldfield TJ, Smerdon SJ, Dauter Z, Petratos K, Wilson KS, Wilkinson AJ, Biochemistry. 1992 Sep 22;31(37):8732-9. PMID:1390659

Page seeded by OCA on Tue Jul 29 13:01:56 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1myi"
Personal tools