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.


2eku

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2eku.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2eku.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2eku| PDB=2eku | SCENE= }}
{{STRUCTURE_2eku| PDB=2eku | SCENE= }}
-
'''Crystal structure of myoglobin reconstituted with 7-methyl-7-depropionatehemin'''
+
===Crystal structure of myoglobin reconstituted with 7-methyl-7-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 02:41:52 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 14:27:55 2008''

Revision as of 11:27, 27 July 2008

Image:2eku.png

Template:STRUCTURE 2eku

Crystal structure of myoglobin reconstituted with 7-methyl-7-depropionatehemin

Template:ABSTRACT PUBMED 17636874

About this Structure

2EKU 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 Sun Jul 27 14:27:55 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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