1fx7

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(New page: 200px<br /><applet load="1fx7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fx7, resolution 2.00&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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'''CRYSTAL STRUCTURE OF THE IRON-DEPENDENT REGULATOR (IDER) FROM MYCOBACTERIUM TUBERCULOSIS'''<br />
'''CRYSTAL STRUCTURE OF THE IRON-DEPENDENT REGULATOR (IDER) FROM MYCOBACTERIUM TUBERCULOSIS'''<br />
==Overview==
==Overview==
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Iron-dependent regulators are primary transcriptional regulators of, virulence factors and iron scavenging systems that are important for, infection by several bacterial pathogens. Here we present the 2.0-A, crystal structure of the wild type iron-dependent regulator from, Mycobacterium tuberculosis in its fully active holorepressor conformation., Clear, unbiased electron density for the Src homology domain 3-like third, domain, which is often invisible in structures of iron-dependent, regulators, was revealed by density modification and averaging. This, domain is one of the rare examples of Src homology domain 3-like folds in, bacterial proteins, and, in addition, displays a metal binding function by, contributing two ligands, one Glu and one Gln, to the pentacoordinated, cobalt atom at metal site 1. Both metal sites are fully occupied, and, tightly bound water molecules at metal site 1 ("Water 1") and metal site 2, ("Water 2") are identified unambiguously. The main chain carbonyl of Leu4, makes an indirect interaction with the cobalt atom at metal site 2 via, Water 2, and the adjacent residue, Val5, forms a rare gamma turn. Residues, 1-3 are well ordered and make numerous interactions. These ordered solvent, molecules and the conformation and interactions of the N-terminal, pentapeptide thus might be important in metal-dependent activation.
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Iron-dependent regulators are primary transcriptional regulators of virulence factors and iron scavenging systems that are important for infection by several bacterial pathogens. Here we present the 2.0-A crystal structure of the wild type iron-dependent regulator from Mycobacterium tuberculosis in its fully active holorepressor conformation. Clear, unbiased electron density for the Src homology domain 3-like third domain, which is often invisible in structures of iron-dependent regulators, was revealed by density modification and averaging. This domain is one of the rare examples of Src homology domain 3-like folds in bacterial proteins, and, in addition, displays a metal binding function by contributing two ligands, one Glu and one Gln, to the pentacoordinated cobalt atom at metal site 1. Both metal sites are fully occupied, and tightly bound water molecules at metal site 1 ("Water 1") and metal site 2 ("Water 2") are identified unambiguously. The main chain carbonyl of Leu4 makes an indirect interaction with the cobalt atom at metal site 2 via Water 2, and the adjacent residue, Val5, forms a rare gamma turn. Residues 1-3 are well ordered and make numerous interactions. These ordered solvent molecules and the conformation and interactions of the N-terminal pentapeptide thus might be important in metal-dependent activation.
==About this Structure==
==About this Structure==
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1FX7 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 SO4 and CO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FX7 OCA].
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1FX7 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=SO4:'>SO4</scene> and <scene name='pdbligand=CO:'>CO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FX7 OCA].
==Reference==
==Reference==
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[[Category: Mycobacterium tuberculosis]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Feese, M.D.]]
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[[Category: Feese, M D.]]
[[Category: Goranson-Siekierke, J.]]
[[Category: Goranson-Siekierke, J.]]
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[[Category: Hol, W.J.G.]]
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[[Category: Hol, W J.G.]]
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[[Category: Holmes, R.K.]]
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[[Category: Holmes, R K.]]
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[[Category: Ingason, B.P.]]
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[[Category: Ingason, B P.]]
[[Category: CO]]
[[Category: CO]]
[[Category: SO4]]
[[Category: SO4]]
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[[Category: mycobacterium tuberculosis]]
[[Category: mycobacterium tuberculosis]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:25:33 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:43:36 2008''

Revision as of 10:43, 21 February 2008


1fx7, resolution 2.00Å

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CRYSTAL STRUCTURE OF THE IRON-DEPENDENT REGULATOR (IDER) FROM MYCOBACTERIUM TUBERCULOSIS

Overview

Iron-dependent regulators are primary transcriptional regulators of virulence factors and iron scavenging systems that are important for infection by several bacterial pathogens. Here we present the 2.0-A crystal structure of the wild type iron-dependent regulator from Mycobacterium tuberculosis in its fully active holorepressor conformation. Clear, unbiased electron density for the Src homology domain 3-like third domain, which is often invisible in structures of iron-dependent regulators, was revealed by density modification and averaging. This domain is one of the rare examples of Src homology domain 3-like folds in bacterial proteins, and, in addition, displays a metal binding function by contributing two ligands, one Glu and one Gln, to the pentacoordinated cobalt atom at metal site 1. Both metal sites are fully occupied, and tightly bound water molecules at metal site 1 ("Water 1") and metal site 2 ("Water 2") are identified unambiguously. The main chain carbonyl of Leu4 makes an indirect interaction with the cobalt atom at metal site 2 via Water 2, and the adjacent residue, Val5, forms a rare gamma turn. Residues 1-3 are well ordered and make numerous interactions. These ordered solvent molecules and the conformation and interactions of the N-terminal pentapeptide thus might be important in metal-dependent activation.

About this Structure

1FX7 is a Single protein structure of sequence from Mycobacterium tuberculosis with and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of the iron-dependent regulator from Mycobacterium tuberculosis at 2.0-A resolution reveals the Src homology domain 3-like fold and metal binding function of the third domain., Feese MD, Ingason BP, Goranson-Siekierke J, Holmes RK, Hol WG, J Biol Chem. 2001 Feb 23;276(8):5959-66. Epub 2000 Oct 26. PMID:11053439

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