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2qj3

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(New page: 200px<br /><applet load="2qj3" size="350" color="white" frame="true" align="right" spinBox="true" caption="2qj3, resolution 3.00&Aring;" /> '''Mycobacterium tuberc...)
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==Overview==
==Overview==
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Mycobacteria display a unique and unusual cell-wall architecture, central, to which is the membrane-proximal mycolyl-arabinogalactan-peptidoglycan, core (mAGP). The biosynthesis of mycolic acids, which form the outermost, layer of the mAGP core, involves malonyl-CoA:acyl carrier protein, transacylase (MCAT). This essential enzyme catalyses the transfer of, malonyl from coenzyme A to acyl carrier protein AcpM, thus feeding these, two-carbon units into the chain-elongation cycle of the type II fatty-acid, synthase. The crystal structure of M. tuberculosis mtFabD, the, mycobacterial MCAT, has been determined to 3.0 A resolution by, multi-wavelength anomalous dispersion. Phasing was facilitated by Ni2+, ions bound to the 20-residue N-terminal affinity tag, which packed between, the two independent copies of mtFabD.
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Mycobacteria display a unique and unusual cell-wall architecture, central to which is the membrane-proximal mycolyl-arabinogalactan-peptidoglycan core (mAGP). The biosynthesis of mycolic acids, which form the outermost layer of the mAGP core, involves malonyl-CoA:acyl carrier protein transacylase (MCAT). This essential enzyme catalyses the transfer of malonyl from coenzyme A to acyl carrier protein AcpM, thus feeding these two-carbon units into the chain-elongation cycle of the type II fatty-acid synthase. The crystal structure of M. tuberculosis mtFabD, the mycobacterial MCAT, has been determined to 3.0 A resolution by multi-wavelength anomalous dispersion. Phasing was facilitated by Ni2+ ions bound to the 20-residue N-terminal affinity tag, which packed between the two independent copies of mtFabD.
==About this Structure==
==About this Structure==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: [Acyl-carrier-protein] S-malonyltransferase]]
[[Category: [Acyl-carrier-protein] S-malonyltransferase]]
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[[Category: Besra, G.S.]]
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[[Category: Besra, G S.]]
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[[Category: Brown, A.K.]]
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[[Category: Brown, A K.]]
[[Category: Futterer, K.]]
[[Category: Futterer, K.]]
[[Category: Ghadbane, H.]]
[[Category: Ghadbane, H.]]
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[[Category: transferase]]
[[Category: transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:20:21 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:39:50 2008''

Revision as of 16:39, 21 February 2008


2qj3, resolution 3.00Å

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Mycobacterium tuberculosis FabD

Overview

Mycobacteria display a unique and unusual cell-wall architecture, central to which is the membrane-proximal mycolyl-arabinogalactan-peptidoglycan core (mAGP). The biosynthesis of mycolic acids, which form the outermost layer of the mAGP core, involves malonyl-CoA:acyl carrier protein transacylase (MCAT). This essential enzyme catalyses the transfer of malonyl from coenzyme A to acyl carrier protein AcpM, thus feeding these two-carbon units into the chain-elongation cycle of the type II fatty-acid synthase. The crystal structure of M. tuberculosis mtFabD, the mycobacterial MCAT, has been determined to 3.0 A resolution by multi-wavelength anomalous dispersion. Phasing was facilitated by Ni2+ ions bound to the 20-residue N-terminal affinity tag, which packed between the two independent copies of mtFabD.

About this Structure

2QJ3 is a Single protein structure of sequence from Mycobacterium tuberculosis with as ligand. Active as [Acyl-carrier-protein_S-malonyltransferase [Acyl-carrier-protein] S-malonyltransferase], with EC number 2.3.1.39 Full crystallographic information is available from OCA.

Reference

Structure of Mycobacterium tuberculosis mtFabD, a malonyl-CoA:acyl carrier protein transacylase (MCAT)., Ghadbane H, Brown AK, Kremer L, Besra GS, Futterer K, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Oct 1;63(Pt, 10):831-5. Epub 2007 Sep 19. PMID:17909282[[Category: [Acyl-carrier-protein] S-malonyltransferase]]

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