1idr

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(New page: 200px<br /> <applet load="1idr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1idr, resolution 1.9&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1idr.jpg|left|200px]]<br /><applet load="1idr" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1idr" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1idr, resolution 1.9&Aring;" />
caption="1idr, resolution 1.9&Aring;" />
'''CRYSTAL STRUCTURE OF THE TRUNCATED-HEMOGLOBIN-N FROM MYCOBACTERIUM TUBERCULOSIS'''<br />
'''CRYSTAL STRUCTURE OF THE TRUNCATED-HEMOGLOBIN-N FROM MYCOBACTERIUM TUBERCULOSIS'''<br />
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==About this Structure==
==About this Structure==
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1IDR 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 PO4, HEM and OXY as [http://en.wikipedia.org/wiki/ligands ligands]. 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IDR OCA].
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1IDR 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=PO4:'>PO4</scene>, <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=OXY:'>OXY</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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==
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[[Category: truncated hemoglobin fold]]
[[Category: truncated hemoglobin fold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Thu Nov 8 13:09:05 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:01:00 2008''

Revision as of 14:01, 15 February 2008


1idr, resolution 1.9Å

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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 with , and as ligands. 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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