1o75: Difference between revisions
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[[Image:1o75.gif|left|200px]]<br /> | [[Image:1o75.gif|left|200px]]<br /><applet load="1o75" size="450" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="1o75" size="450" color="white" frame="true" align="right" spinBox="true" | |||
caption="1o75, resolution 1.95Å" /> | caption="1o75, resolution 1.95Å" /> | ||
'''TP47, THE 47-KILODALTON LIPOPROTEIN OF TREPONEMA PALLIDUM'''<br /> | '''TP47, THE 47-KILODALTON LIPOPROTEIN OF TREPONEMA PALLIDUM'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1O75 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Treponema_pallidum Treponema pallidum] with XE and PDX as [http://en.wikipedia.org/wiki/ligands ligands]. | 1O75 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Treponema_pallidum Treponema pallidum] with XE and PDX as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Xe Binding Site For Chain B'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1O75 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: penicillin-binding protein]] | [[Category: penicillin-binding protein]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 16:53:07 2007'' | ||
Revision as of 17:43, 18 December 2007
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TP47, THE 47-KILODALTON LIPOPROTEIN OF TREPONEMA PALLIDUM
OverviewOverview
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 to other PBPs. It comprises four distinct domains: two complex, beta-sheet-containing N-terminal domains and two C-terminal domains that, adopt immunoglobulin-like folds. The three hypothetical PBP signature, motifs do not come together to form a typical PBP active site., Furthermore, Tp47 is unusual in that it displays beta-lactamase activity, (k(cat) for penicillin = 271 +/- 6 s(-1)), a feature that hindered, attempts to identify the active site in Tp47 by co-crystallization and, mass spectrometric techniques. Taken together, Tp47 does not fit the, classical structural and mechanistic paradigms for PBPs, and thus Tp47, appears to represent a new class of PBP.
About this StructureAbout this Structure
1O75 is a Single protein structure of sequence from Treponema pallidum with XE and PDX as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
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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