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.


1obm

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1obm.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1obm.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1obm| PDB=1obm | SCENE= }}
{{STRUCTURE_1obm| PDB=1obm | SCENE= }}
-
'''RECOMBINANT SPERM WHALE MYOGLOBIN 29F/64Q/68F/122N MUTANT (MET)'''
+
===RECOMBINANT SPERM WHALE MYOGLOBIN 29F/64Q/68F/122N MUTANT (MET)===
-
==Overview==
+
<!--
-
The bivalve mollusc Lucina pectinata harbors sulfide-oxidizing chemoautotrophic bacteria and expresses a monomeric hemoglobin I, HbI, with normal O2, but extraordinarily high sulfide affinity. The crystal structure of aquomet Lucina HbI has revealed an active site with three residues not commonly found in vertebrate globins: Phe(B10), Gln(E7), and Phe(E11) (Rizzi, M., Wittenberg, J. B., Coda, A., Fasano, M., Ascenzi, P., and Bolognesi, M. (1994) J. Mol. Biol. 244, 86-89). Engineering these three residues into sperm whale myoglobin results in a triple mutant with approximately 700-fold higher sulfide affinity than for wild-type. The single crystal x-ray structure of the aquomet derivative of the myoglobin triple mutant and the solution 1H NMR active site structures of the cyanomet derivatives of both the myoglobin mutant and Lucina HbI have been determined to examine further the structural origin of their unusually high sulfide affinities. The major differences in the distal pocket is that in the aquomet form the carbonyl of Gln64(E7) serves as a H-bond acceptor, whereas in the cyanomet form the amido group acts as H-bond donor to the bound ligand. Phe68(E11) is rotated approximately 90 degrees about chi2 and located approximately 1-2 A closer to the iron atom in the myoglobin triple mutant relative to its conformation in Lucina HbI. The change in orientation potentially eliminates the stabilizing interaction with sulfide and, together with the decrease in size of the distal pocket, accounts for the 7-fold lower sulfide affinity of the myoglobin mutant compared with that of Lucina HbI.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9545280}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9545280 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9545280}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Oxygen binding muscle protein]]
[[Category: Oxygen binding muscle protein]]
[[Category: Oxygen transport]]
[[Category: Oxygen transport]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:38:11 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 21:23:34 2008''

Revision as of 18:23, 28 July 2008

Image:1obm.png

Template:STRUCTURE 1obm

RECOMBINANT SPERM WHALE MYOGLOBIN 29F/64Q/68F/122N MUTANT (MET)

Template:ABSTRACT PUBMED 9545280

About this Structure

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

Reference

Solution and crystal structures of a sperm whale myoglobin triple mutant that mimics the sulfide-binding hemoglobin from Lucina pectinata., Nguyen BD, Zhao X, Vyas K, La Mar GN, Lile RA, Brucker EA, Phillips GN Jr, Olson JS, Wittenberg JB, J Biol Chem. 1998 Apr 17;273(16):9517-26. PMID:9545280

Page seeded by OCA on Mon Jul 28 21:23:34 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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