1qmf
From Proteopedia
(Difference between revisions)
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| - | [[Image:1qmf.png|left|200px]] | ||
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{{STRUCTURE_1qmf| PDB=1qmf | SCENE= }} | {{STRUCTURE_1qmf| PDB=1qmf | SCENE= }} | ||
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===PENICILLIN-BINDING PROTEIN 2X (PBP-2X) ACYL-ENZYME COMPLEX=== | ===PENICILLIN-BINDING PROTEIN 2X (PBP-2X) ACYL-ENZYME COMPLEX=== | ||
| + | {{ABSTRACT_PUBMED_10860753}} | ||
| - | + | ==Function== | |
| + | [[http://www.uniprot.org/uniprot/PBPX_STRPN PBPX_STRPN]] Penicillin-binding proteins (PBPs) function in the late steps of murein biosynthesis. Beta-lactams inactivate the PBPs by acylating an essential serine residue in the active site of these proteins. | ||
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID:010860753</ref><ref group="xtra">PMID:008605631</ref><ref group="xtra">PMID:008355266</ref><ref group="xtra">PMID:018234221</ref><references group="xtra"/> | + | <ref group="xtra">PMID:010860753</ref><ref group="xtra">PMID:008605631</ref><ref group="xtra">PMID:008355266</ref><ref group="xtra">PMID:018234221</ref><references group="xtra"/><references/> |
[[Category: Streptococcus pneumoniae]] | [[Category: Streptococcus pneumoniae]] | ||
[[Category: Dideberg, O.]] | [[Category: Dideberg, O.]] | ||
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[[Category: Gordon, E J.]] | [[Category: Gordon, E J.]] | ||
[[Category: Mouz, N.]] | [[Category: Mouz, N.]] | ||
| + | [[Category: Cell cycle]] | ||
[[Category: Cell wall]] | [[Category: Cell wall]] | ||
[[Category: Peptidoglycan synthesis]] | [[Category: Peptidoglycan synthesis]] | ||
| - | [[Category: Resistance]] | ||
| - | [[Category: Transmembrane]] | ||
Revision as of 19:26, 17 April 2013
Contents |
PENICILLIN-BINDING PROTEIN 2X (PBP-2X) ACYL-ENZYME COMPLEX
Template:ABSTRACT PUBMED 10860753
Function
[PBPX_STRPN] Penicillin-binding proteins (PBPs) function in the late steps of murein biosynthesis. Beta-lactams inactivate the PBPs by acylating an essential serine residue in the active site of these proteins.
About this Structure
1qmf is a 1 chain structure with sequence from Streptococcus pneumoniae. Full crystallographic information is available from OCA.
See Also
Reference
- Gordon E, Mouz N, Duee E, Dideberg O. The crystal structure of the penicillin-binding protein 2x from Streptococcus pneumoniae and its acyl-enzyme form: implication in drug resistance. J Mol Biol. 2000 Jun 2;299(2):477-85. PMID:10860753 doi:10.1006/jmbi.2000.3740
- Pares S, Mouz N, Petillot Y, Hakenbeck R, Dideberg O. X-ray structure of Streptococcus pneumoniae PBP2x, a primary penicillin target enzyme. Nat Struct Biol. 1996 Mar;3(3):284-9. PMID:8605631
- Charlier P, Buisson G, Dideberg O, Wierenga J, Keck W, Laible G, Hakenbeck R. Crystallization of a genetically engineered water-soluble primary penicillin target enzyme. The high molecular mass PBP2x of Streptococcus pneumoniae. J Mol Biol. 1993 Aug 5;232(3):1007-9. PMID:8355266 doi:http://dx.doi.org/S0022-2836(83)71452-X
- Maurer P, Koch B, Zerfass I, Krauss J, van der Linden M, Frere JM, Contreras-Martel C, Hakenbeck R. Penicillin-binding protein 2x of Streptococcus pneumoniae: three new mutational pathways for remodelling an essential enzyme into a resistance determinant. J Mol Biol. 2008 Mar 7;376(5):1403-16. Epub 2008 Jan 4. PMID:18234221 doi:10.1016/j.jmb.2007.12.058
