2gkn
From Proteopedia
(New page: 200px<br /> <applet load="2gkn" size="450" color="white" frame="true" align="right" spinBox="true" caption="2gkn, resolution 2.10Å" /> '''Crystal structure o...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:2gkn.gif|left|200px]]<br /> | + | [[Image:2gkn.gif|left|200px]]<br /><applet load="2gkn" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2gkn" size=" | + | |
caption="2gkn, resolution 2.10Å" /> | caption="2gkn, resolution 2.10Å" /> | ||
'''Crystal structure of Mycobacterium tuberculosis trHbN, GlnE11Val mutant'''<br /> | '''Crystal structure of Mycobacterium tuberculosis trHbN, GlnE11Val mutant'''<br /> | ||
| Line 8: | Line 7: | ||
==About this Structure== | ==About this Structure== | ||
| - | 2GKN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with NA, CYN and HEM as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 2GKN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=CYN:'>CYN</scene> and <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GKN OCA]. |
==Reference== | ==Reference== | ||
| Line 21: | Line 20: | ||
[[Category: truncated hemoglobin; mutant]] | [[Category: truncated hemoglobin; mutant]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:28:22 2008'' |
Revision as of 15:28, 15 February 2008
|
Crystal structure of Mycobacterium tuberculosis trHbN, GlnE11Val 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.
About this Structure
2GKN is a Single protein structure of sequence from Mycobacterium tuberculosis with , and as ligands. 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 Fri Feb 15 17:28:22 2008
