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1o75
From Proteopedia
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Revision as of 13:40, 30 October 2007
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TP47, THE 47-KILODALTON LIPOPROTEIN OF TREPONEMA PALLIDUM
Overview
Syphilis is a complex sexually transmitted disease caused by the, spirochetal bacterium Treponema pallidum. T. pallidum has remained, exquisitely sensitive to penicillin, but the mode of action and lethal, targets for beta-lactams are still unknown. We previously identified the, T. pallidum 47-kDa lipoprotein (Tp47) as a penicillin-binding protein, (PBP). Tp47 contains three hypothetical consensus motifs (SVTK, TEN, and, KTG) that typically form the active center of other PBPs. Yet, in this, study, mutations of key amino acids within these motifs failed to abolish, the penicillin binding activity of Tp47. The crystal structure of Tp47 at, a resolution of 1.95 A revealed a fold different from any other known PBP;, Tp47 is predominantly beta-sheet, in contrast to the alpha/beta-fold, common ... [(full description)]
About this Structure
1O75 is a [Single protein] structure of sequence from [Treponema pallidum] with XE and PDX as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Crystal structure of the 47-kDa lipoprotein of Treponema pallidum reveals a novel penicillin-binding protein., Deka RK, Machius M, Norgard MV, Tomchick DR, J Biol Chem. 2002 Nov 1;277(44):41857-64. Epub 2002 Aug 24. PMID:12196546
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