1idr
From Proteopedia
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|PDB= 1idr |SIZE=350|CAPTION= <scene name='initialview01'>1idr</scene>, resolution 1.9Å | |PDB= 1idr |SIZE=350|CAPTION= <scene name='initialview01'>1idr</scene>, resolution 1.9Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1idr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1idr OCA], [http://www.ebi.ac.uk/pdbsum/1idr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1idr RCSB]</span> | ||
}} | }} | ||
| Line 28: | Line 31: | ||
[[Category: Milani, M.]] | [[Category: Milani, M.]] | ||
[[Category: Pesce, A.]] | [[Category: Pesce, A.]] | ||
| - | [[Category: HEM]] | ||
| - | [[Category: OXY]] | ||
| - | [[Category: PO4]] | ||
[[Category: truncated hemoglobin fold]] | [[Category: truncated hemoglobin fold]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:18:21 2008'' |
Revision as of 18:18, 30 March 2008
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| , resolution 1.9Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE TRUNCATED-HEMOGLOBIN-N FROM MYCOBACTERIUM TUBERCULOSIS
Overview
Macrophage-generated oxygen- and nitrogen-reactive species control the development of Mycobacterium tuberculosis infection in the host. Mycobacterium tuberculosis 'truncated hemoglobin' N (trHbN) has been related to nitric oxide (NO) detoxification, in response to macrophage nitrosative stress, during the bacterium latent infection stage. The three-dimensional structure of oxygenated trHbN, solved at 1.9 A resolution, displays the two-over-two alpha-helical sandwich fold recently characterized in two homologous truncated hemoglobins, featuring an extra N-terminal alpha-helix and homodimeric assembly. In the absence of a polar distal E7 residue, the O2 heme ligand is stabilized by two hydrogen bonds to TyrB10(33). Strikingly, ligand diffusion to the heme in trHbN may occur via an apolar tunnel/cavity system extending for approximately 28 A through the protein matrix, connecting the heme distal cavity to two distinct protein surface sites. This unique structural feature appears to be conserved in several homologous truncated hemoglobins. It is proposed that in trHbN, heme Fe/O2 stereochemistry and the protein matrix tunnel may promote O2/NO chemistry in vivo, as a M.tuberculosis defense mechanism against macrophage nitrosative stress.
About this Structure
1IDR is a Single protein structure of sequence from Mycobacterium tuberculosis. The following page contains interesting information on the relation of 1IDR with [Hemoglobin]. Full crystallographic information is available from OCA.
Reference
Mycobacterium tuberculosis hemoglobin N displays a protein tunnel suited for O2 diffusion to the heme., Milani M, Pesce A, Ouellet Y, Ascenzi P, Guertin M, Bolognesi M, EMBO J. 2001 Aug 1;20(15):3902-9. PMID:11483493
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