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| - | [[Image:1w92.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1w92.png|left|200px]] |
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| | {{STRUCTURE_1w92| PDB=1w92 | SCENE= }} | | {{STRUCTURE_1w92| PDB=1w92 | SCENE= }} |
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| - | '''THE STRUCTURE OF CARBOMONOXY MURINE NEUROGLOBIN REVEALS A HEME-SLIDING MECHANISM FOR AFFINITY REGULATION'''
| + | ===THE STRUCTURE OF CARBOMONOXY MURINE NEUROGLOBIN REVEALS A HEME-SLIDING MECHANISM FOR AFFINITY REGULATION=== |
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| - | ==Overview==
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| - | Neuroglobin (Ngb), a globular heme protein expressed in the brain of vertebrates, binds oxygen reversibly, with an affinity comparable to myoglobin (Mb). Despite low sequence identity, the overall 3D fold of Ngb and Mb is very similar. Unlike in Mb, in Ngb the sixth coordination position of the heme iron is occupied by the distal histidine, in the absence of an exogenous ligand. Endogenous ligation has been proposed as a unique mechanism for affinity regulation and ligand discrimination in heme proteins. This peculiarity might be related to the still-unknown physiological function of Ngb. Here, we present the x-ray structure of CO-bound ferrous murine Ngb at 1.7 A and a comparison with the 1.5-A structure of ferric bis-histidine Ngb. We have also used Fourier transform IR spectroscopy of WT and mutant CO-ligated Ngb to examine structural heterogeneity in the active site. Upon CO binding, the distal histidine retains (by and large) its position, whereas the heme group slides deeper into a preformed crevice, thereby reshaping the large cavity ( approximately 290 A(3)) connecting the distal and proximal heme sides with the bulk. The heme relocation is accompanied by a significant decrease of structural disorder, especially of the EF loop, which may be the signal whereby Ngb communicates hypoxic conditions. This unexpected structural change unveils a heme-sliding mechanism of affinity control that may be of significance to understanding Ngb's role in the pathophysiology of the brain.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15548613}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15548613 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15548613}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Heme-sliding]] | | [[Category: Heme-sliding]] |
| | [[Category: Oxygen storage/transport]] | | [[Category: Oxygen storage/transport]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:19:37 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:23:34 2008'' |
Revision as of 16:23, 27 July 2008
Template:STRUCTURE 1w92
THE STRUCTURE OF CARBOMONOXY MURINE NEUROGLOBIN REVEALS A HEME-SLIDING MECHANISM FOR AFFINITY REGULATION
Template:ABSTRACT PUBMED 15548613
About this Structure
1W92 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
The structure of carbonmonoxy neuroglobin reveals a heme-sliding mechanism for control of ligand affinity., Vallone B, Nienhaus K, Matthes A, Brunori M, Nienhaus GU, Proc Natl Acad Sci U S A. 2004 Dec 14;101(50):17351-6. Epub 2004 Nov 17. PMID:15548613
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