1o75
From Proteopedia
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|PDB= 1o75 |SIZE=350|CAPTION= <scene name='initialview01'>1o75</scene>, resolution 1.95Å | |PDB= 1o75 |SIZE=350|CAPTION= <scene name='initialview01'>1o75</scene>, resolution 1.95Å | ||
|SITE= <scene name='pdbsite=AC1:Xe+Binding+Site+For+Chain+B'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Xe+Binding+Site+For+Chain+B'>AC1</scene> | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=PDX:2,3-DI-O-SULFO-ALPHA-D-GLUCOPYRANOSE'>PDX</scene>, <scene name='pdbligand=XE:XENON'>XE</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1o75 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o75 OCA], [http://www.ebi.ac.uk/pdbsum/1o75 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1o75 RCSB]</span> | ||
}} | }} | ||
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[[Category: Norgard, M V.]] | [[Category: Norgard, M V.]] | ||
[[Category: Tomchick, D R.]] | [[Category: Tomchick, D R.]] | ||
| - | [[Category: PDX]] | ||
| - | [[Category: XE]] | ||
[[Category: antigen]] | [[Category: antigen]] | ||
[[Category: four-domain protein]] | [[Category: four-domain protein]] | ||
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[[Category: penicillin-binding protein]] | [[Category: penicillin-binding protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:40:50 2008'' |
Revision as of 19:40, 30 March 2008
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| , resolution 1.95Å | |||||||
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| Sites: | |||||||
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 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 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
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