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| - | [[Image:1o75.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1o75.png|left|200px]] |
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| | {{STRUCTURE_1o75| PDB=1o75 | SCENE= }} | | {{STRUCTURE_1o75| PDB=1o75 | SCENE= }} |
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| - | '''TP47, THE 47-KILODALTON LIPOPROTEIN OF TREPONEMA PALLIDUM'''
| + | ===TP47, THE 47-KILODALTON LIPOPROTEIN OF TREPONEMA PALLIDUM=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_12196546}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 12196546 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_12196546}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Lipoprotein]] | | [[Category: Lipoprotein]] |
| | [[Category: Penicillin-binding protein]] | | [[Category: Penicillin-binding protein]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:28:00 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:02:08 2008'' |
Revision as of 01:02, 28 July 2008
Template:STRUCTURE 1o75
TP47, THE 47-KILODALTON LIPOPROTEIN OF TREPONEMA PALLIDUM
Template:ABSTRACT PUBMED 12196546
About this Structure
1O75 is a Single protein structure of sequence from Treponema pallidum. 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
Page seeded by OCA on Mon Jul 28 04:02:08 2008
