We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

2ekt

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2ekt.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2ekt.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2ekt| PDB=2ekt | SCENE= }}
{{STRUCTURE_2ekt| PDB=2ekt | SCENE= }}
-
'''Crystal structure of myoglobin reconstituted with 6-methyl-6-depropionatehemin'''
+
===Crystal structure of myoglobin reconstituted with 6-methyl-6-depropionatehemin===
-
==Overview==
+
<!--
-
Two heme propionate side chains, which are attached at the 6 and 7 positions of the heme framework, are linked with Arg45 and Ser92, respectively, in sperm whale myoglobin. To evaluate the role of each propionate, two kinds of one-legged hemins, 6-depropionated and 7-depropionated protohemins, were prepared and inserted into the apomyoglobin to yield two reconstituted proteins. Structural data of the reconstituted myoglobins were obtained via an X-ray crystallographic analysis at a resolution of 1.1-1.4 A and resonance Raman spectroscopy. It was found that the lack of the 6-propionate reduces the number of hydrogen bonds in the distal site and clearly changes the position of the Arg45 residue with the disrupting Arg45-Asp60 interaction. In contrast, the removal of the 7-propionate does not cause a significant structural change in the residues of the distal and proximal sites. However, the resonance Raman studies suggested that the coordination bond strength of the His93-Fe bond for the protein with the 7-depropionated protoheme slightly increases compared to that for the protein with the native heme. The O2 and CO ligand binding studies for the reconstituted proteins with the one-legged hemes provide an important insight into the functional role of each propionate. The lack of the 6-propionate accelerates the O2 dissociation by ca. 3-fold compared to those of the other reconstituted and native proteins. The lack of the 7-propionate enhances the CO affinity by 2-fold compared to that of the protein with the native heme. These results indicate that the 6-propionate clearly contributes to the stabilization of the bound O2, whereas the 7-propionate plays an important role in the regulation of the Fe-His bond.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17636874}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17636874 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17636874}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Globin fold]]
[[Category: Globin fold]]
[[Category: Oxygen storage/transport complex]]
[[Category: Oxygen storage/transport complex]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 02:41:51 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 05:38:45 2008''

Revision as of 02:38, 28 July 2008

Image:2ekt.png

Template:STRUCTURE 2ekt

Crystal structure of myoglobin reconstituted with 6-methyl-6-depropionatehemin

Template:ABSTRACT PUBMED 17636874

About this Structure

2EKT is a Single protein structure of sequence from Physeter catodon. Full crystallographic information is available from OCA.

Reference

Structure and ligand binding properties of myoglobins reconstituted with monodepropionated heme: functional role of each heme propionate side chain., Harada K, Makino M, Sugimoto H, Hirota S, Matsuo T, Shiro Y, Hisaeda Y, Hayashi T, Biochemistry. 2007 Aug 21;46(33):9406-16. Epub 2007 Jul 18. PMID:17636874

Page seeded by OCA on Mon Jul 28 05:38:45 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2ekt"
Personal tools