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.


2oh9

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2oh9.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2oh9.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2oh9| PDB=2oh9 | SCENE= }}
{{STRUCTURE_2oh9| PDB=2oh9 | SCENE= }}
-
'''Myoglobin cavity mutant V68W'''
+
===Myoglobin cavity mutant V68W===
-
==Overview==
+
<!--
-
The pathways for ligand entry and exit in myoglobin have now been well established by a wide variety of experimental results, including pico- to nano- to microsecond transient absorbance measurements and time-resolved X-ray crystallographic measurements. Trp insertions have been used to block, one at a time, the three major cavities occupied by photodissociated ligands. In this work, we review the effects of the L29(B10)W mutation, which places a large indole ring in the initial 'docking site' for photodissociated ligands. Then, the effects of blocking the Xe4 site with I28W, V68W, and I107W mutations and the Xe1 cavity with L89W, L104W, and F138W mutations are described. The structures of four of these mutants are shown for the first time (Trp28, Trp68, Trp107, and Trp 138 sperm whale metMb). All available results support a 'side path' mechanism in which ligands move into and out of myoglobin by outward rotation of the HisE7 side chain, but after entry can migrate into internal cavities, including the distal Xe4 and proximal Xe1 binding sites. The distal cavities act like the pocket of a baseball glove, catching the ligand and holding it long enough for the histidine gate to close and facilitate internal coordination with the heme iron atom. The physiological role of the proximal Xe1 site is less clear because changes in the size of this cavity have minimal effects on overall O(2) binding parameters.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17701550}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17701550 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17701550}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Ligand entry and exit pathway]]
[[Category: Ligand entry and exit pathway]]
[[Category: Myoglobin]]
[[Category: Myoglobin]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 10:54:59 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 21:36:28 2008''

Revision as of 18:36, 27 July 2008

Image:2oh9.png

Template:STRUCTURE 2oh9

Myoglobin cavity mutant V68W

Template:ABSTRACT PUBMED 17701550

About this Structure

2OH9 is a Single protein structure of sequence from Physeter catodon. Full crystallographic information is available from OCA.

Reference

Ligand pathways in myoglobin: a review of Trp cavity mutations., Olson JS, Soman J, Phillips GN Jr, IUBMB Life. 2007 Aug-Sep;59(8-9):552-62. PMID:17701550

Page seeded by OCA on Sun Jul 27 21:36:28 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2oh9"
Personal tools