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.


2gkm

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2gkm.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2gkm.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2gkm| PDB=2gkm | SCENE= }}
{{STRUCTURE_2gkm| PDB=2gkm | SCENE= }}
-
'''Crystal structure of Mycobacterium tuberculosis trHbN TyrB10Phe mutant'''
+
===Crystal structure of Mycobacterium tuberculosis trHbN TyrB10Phe mutant===
-
==Overview==
+
<!--
-
The crystallographic structure of oxygenated trHbN from Mycobacterium tuberculosis showed an extended heme distal site hydrogen-bonding network that includes Y(B10), Q(E11), and the bound O(2) (Milani, M., et al. (2001) EMBO J. 20, 3902-3909). In the present work, we analyze the effects that substitutions at the B10 and E11 positions exert on the heme and its coordinated ligands, using steady-state resonance Raman spectroscopy, absorption spectroscopy and X-ray crystallography. Our results show that (1) residues Y(B10) and Q(E11) control the binding and the ionization state of the heme-bound water molecules in ferric trHbN and are important in keeping the sixth coordination position vacant in deoxy trHbN; (2) residue Q(E11) plays a role in maintaining the integrity of the proximal Fe-His bond in deoxy trHbN; (3) in wild-type oxy-trHbN, the size and hydrogen-bonding capability of residue E11 is important to sustain proper interaction between Y(B10) and the heme-bound O(2); (4) CO-trHbN is in a conformational equilibrium, where either the Y(B10) or the Q(E11) residue interacts with the heme-bound CO; and (5) Y(B10) and Q(E11) residues control the conformation (and likely the dynamics) of the protein matrix tunnel gating residue F(E15). These findings suggest that the functional processes of ligand binding and diffusion are controlled in trHbN through the dynamic interaction of residues Y(B10), Q(E11), F(E15), and the heme ligand.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16846220}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16846220 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16846220}}
==About this Structure==
==About this Structure==
Line 26: Line 30:
[[Category: Mutant]]
[[Category: Mutant]]
[[Category: Truncated hemoglobin]]
[[Category: Truncated hemoglobin]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:12:42 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 05:25:39 2008''

Revision as of 02:25, 29 July 2008

Image:2gkm.png

Template:STRUCTURE 2gkm

Crystal structure of Mycobacterium tuberculosis trHbN TyrB10Phe mutant

Template:ABSTRACT PUBMED 16846220

About this Structure

2GKM is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

Reference

Ligand interactions in the distal heme pocket of Mycobacterium tuberculosis truncated hemoglobin N: roles of TyrB10 and GlnE11 residues., Ouellet Y, Milani M, Couture M, Bolognesi M, Guertin M, Biochemistry. 2006 Jul 25;45(29):8770-81. PMID:16846220

Page seeded by OCA on Tue Jul 29 05:25:39 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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