1idr
From Proteopedia
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| - | [[Image:1idr.jpg|left|200px]] | + | [[Image:1idr.jpg|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF THE TRUNCATED-HEMOGLOBIN-N FROM MYCOBACTERIUM TUBERCULOSIS''' | + | {{Structure |
| + | |PDB= 1idr |SIZE=350|CAPTION= <scene name='initialview01'>1idr</scene>, resolution 1.9Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> and <scene name='pdbligand=OXY:OXYGEN MOLECULE'>OXY</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF THE TRUNCATED-HEMOGLOBIN-N FROM MYCOBACTERIUM TUBERCULOSIS''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1IDR is a [ | + | 1IDR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. The following page contains interesting information on the relation of 1IDR with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb41_1.html Hemoglobin]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IDR OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11483493 11483493] |
[[Category: Hemoglobin]] | [[Category: Hemoglobin]] | ||
[[Category: Mycobacterium tuberculosis]] | [[Category: Mycobacterium tuberculosis]] | ||
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[[Category: truncated hemoglobin fold]] | [[Category: truncated hemoglobin fold]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:49:07 2008'' |
Revision as of 09:49, 20 March 2008
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| , resolution 1.9Å | |||||||
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| Ligands: | , and | ||||||
| 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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