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.


1h1x

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1h1x.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1h1x.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1h1x| PDB=1h1x | SCENE= }}
{{STRUCTURE_1h1x| PDB=1h1x | SCENE= }}
-
'''SPERM WHALE MYOGLOBIN MUTANT T67R S92D'''
+
===SPERM WHALE MYOGLOBIN MUTANT T67R S92D===
-
==Overview==
+
<!--
-
Atomic co-ordinates and structure factors for the T67R/S92D metMbCN mutant have been deposited with the Protein Data Bank, under accession codes 1h1x and r1h1xsf, respectively. Protein engineering and cofactor replacement have been employed as tools to introduce/modulate peroxidase activity in sperm whale Mb (myoglobin). Based on the rationale that haem peroxidase active sites are characterized by specific charged residues, the Mb haem crevice has been modified to host a haem-distalpropionate Arg residue and a proximal Asp, yielding the T67R/S92D Mb mutant. To code extra conformational mobility around the haem, and to increase the peroxidase catalytic efficiency, the T67R/S92D Mb mutant has been subsequently reconstituted with protohaem-L-histidine methyl ester, yielding a stable derivative, T67R/S92D Mb-H. The crystal structure of T67R/S92D cyano-metMb (1.4 A resolution; R factor, 0.12) highlights a regular haem-cyanide binding mode, and the role for the mutated residues in affecting the haem propionates as well as the neighbouring water structure. The conformational disorder of the haem propionate-7 is evidenced by the NMR spectrum of the mutant. Ligand-binding studies show that the iron(III) centres of T67R/S92D Mb, and especially of T67R/S92D Mb-H, exhibit higher affinity for azide and imidazole than wild-type Mb. In addition, both protein derivatives react faster than wild-type Mb with hydrogen peroxide, showing higher peroxidase-like activity towards phenolic substrates. The catalytic efficiency of T67R/S92D Mb-H in these reactions is the highest so far reported for Mb derivatives. A model for the protein-substrate interaction is deduced based on the crystal structure and on the NMR spectra of protein-phenol complexes.
+
The line below this paragraph, {{ABSTRACT_PUBMED_14563209}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 14563209 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_14563209}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Oxygen storage]]
[[Category: Oxygen storage]]
[[Category: Peroxidase]]
[[Category: Peroxidase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:18:50 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 06:29:01 2008''

Revision as of 03:29, 1 July 2008

Image:1h1x.png

Template:STRUCTURE 1h1x

SPERM WHALE MYOGLOBIN MUTANT T67R S92D

Template:ABSTRACT PUBMED 14563209

About this Structure

1H1X is a Single protein structure of sequence from Physeter catodon. Full crystallographic information is available from OCA.

Reference

Engineering peroxidase activity in myoglobin: the haem cavity structure and peroxide activation in the T67R/S92D mutant and its derivative reconstituted with protohaemin-l-histidine., Roncone R, Monzani E, Murtas M, Battaini G, Pennati A, Sanangelantoni AM, Zuccotti S, Bolognesi M, Casella L, Biochem J. 2004 Feb 1;377(Pt 3):717-24. PMID:14563209

Page seeded by OCA on Tue Jul 1 06:29:01 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1h1x"
Personal tools