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.


1i4y

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1i4y.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1i4y.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1i4y| PDB=1i4y | SCENE= }}
{{STRUCTURE_1i4y| PDB=1i4y | SCENE= }}
-
'''THE CRYSTAL STRUCTURE OF PHASCOLOPSIS GOULDII WILD TYPE METHEMERYTHRIN'''
+
===THE CRYSTAL STRUCTURE OF PHASCOLOPSIS GOULDII WILD TYPE METHEMERYTHRIN===
-
==Overview==
+
<!--
-
Reported are the X-ray crystal structures of recombinant Phascolopsis gouldii methemerythrin (1.8-A resolution) and the structure of an O2-binding-pocket mutant, L98Y methemerythrin (2.1-A resolution). The L98Y hemerythrin (Hr) has a greatly enhanced O2 affinity, a slower O2 dissociation rate, a larger solvent deuterium isotope effect on this rate, and a greater resistance to autoxidation relative to the wild-type protein. The crystal structures show that the hydrophobic binding pocket of Hr can accommodate substitution of a leucyl by a tyrosyl side chain with relatively minor structural rearrangements. UV/vis and resonance Raman spectra show that in solution L98Y methemerythrin contains a mixture of two diiron site structures differing by the absence or presence of an Fe(III)-coordinated phenolate. However, in the crystal, only one L98Y diiron site structure is seen, in which the Y98 hydroxyl is not a ligand, but instead forms a hydrogen bond to a terminal hydroxo/aqua ligand to the nearest iron. Based on this crystal structure, we propose that in the oxy form of L98Y hemerythrin the non-polar nature of the binding pocket favors localization of the Y98 hydroxyl near the O2 binding site, where it can donate a hydrogen bond to the hydroperoxo ligand. The stabilizing Y98OH-O2H-interaction would account for all of the altered O2 binding properties of L98Y Hr listed above.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11372200}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11372200 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11372200}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Hemerythrin]]
[[Category: Hemerythrin]]
[[Category: Oxygen binding]]
[[Category: Oxygen binding]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:34:47 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 10:25:35 2008''

Revision as of 07:25, 1 July 2008

Image:1i4y.png

Template:STRUCTURE 1i4y

THE CRYSTAL STRUCTURE OF PHASCOLOPSIS GOULDII WILD TYPE METHEMERYTHRIN

Template:ABSTRACT PUBMED 11372200

About this Structure

1I4Y is a Single protein structure of sequence from Phascolopsis gouldii. Full crystallographic information is available from OCA.

Reference

The crystal structures of Phascolopsis gouldii wild type and L98Y methemerythrins: structural and functional alterations of the O2 binding pocket., Farmer CS, Kurtz DM Jr, Liu ZJ, Wang BC, Rose J, Ai J, Sanders-Loehr J, J Biol Inorg Chem. 2001 Apr;6(4):418-29. PMID:11372200

Page seeded by OCA on Tue Jul 1 10:25:35 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1i4y"
Personal tools