2jch

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[[Image:2jch.jpg|left|200px]]<br /><applet load="2jch" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2jch.jpg|left|200px]]
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caption="2jch, resolution 2.40&Aring;" />
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'''STRUCTURAL AND MECHANISTIC BASIS OF PENICILLIN BINDING PROTEIN INHIBITION BY LACTIVICINS'''<br />
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{{Structure
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|PDB= 2jch |SIZE=350|CAPTION= <scene name='initialview01'>2jch</scene>, resolution 2.40&Aring;
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|SITE= <scene name='pdbsite=AC1:Pl7+Binding+Site+For+Chain+A'>AC1</scene>, <scene name='pdbsite=AC2:So4+Binding+Site+For+Chain+A'>AC2</scene>, <scene name='pdbsite=AC3:Cl+Binding+Site+For+Chain+A'>AC3</scene> and <scene name='pdbsite=AC4:Edo+Binding+Site+For+Chain+A'>AC4</scene>
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene> and <scene name='pdbligand=PL7:(2E)-2-({(2S)-2-CARBOXY-2-[(PHENOXYACETYL)AMINO]ETHOXY}IMINO)PENTANEDIOIC ACID'>PL7</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''STRUCTURAL AND MECHANISTIC BASIS OF PENICILLIN BINDING PROTEIN INHIBITION BY LACTIVICINS'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2JCH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_pneumoniae_r6 Streptococcus pneumoniae r6] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=EDO:'>EDO</scene> and <scene name='pdbligand=PL7:'>PL7</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <scene name='pdbsite=AC1:Pl7+Binding+Site+For+Chain+A'>AC1</scene>, <scene name='pdbsite=AC2:So4+Binding+Site+For+Chain+A'>AC2</scene>, <scene name='pdbsite=AC3:Cl+Binding+Site+For+Chain+A'>AC3</scene> and <scene name='pdbsite=AC4:Edo+Binding+Site+For+Chain+A'>AC4</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JCH OCA].
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2JCH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_pneumoniae_r6 Streptococcus pneumoniae r6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JCH OCA].
==Reference==
==Reference==
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Structural and mechanistic basis of penicillin-binding protein inhibition by lactivicins., Macheboeuf P, Fischer DS, Brown T Jr, Zervosen A, Luxen A, Joris B, Dessen A, Schofield CJ, Nat Chem Biol. 2007 Sep;3(9):565-9. Epub 2007 Aug 5. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17676039 17676039]
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Structural and mechanistic basis of penicillin-binding protein inhibition by lactivicins., Macheboeuf P, Fischer DS, Brown T Jr, Zervosen A, Luxen A, Joris B, Dessen A, Schofield CJ, Nat Chem Biol. 2007 Sep;3(9):565-9. Epub 2007 Aug 5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17676039 17676039]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Streptococcus pneumoniae r6]]
[[Category: Streptococcus pneumoniae r6]]
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[[Category: cell wall]]
[[Category: cell wall]]
[[Category: drug-binding protein]]
[[Category: drug-binding protein]]
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[[Category: gamma lactam antibiotics]]
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[[Category: gamma lactam antibiotic]]
[[Category: peptidoglycan]]
[[Category: peptidoglycan]]
[[Category: peptidoglycan synthesis multifunctional enzyme]]
[[Category: peptidoglycan synthesis multifunctional enzyme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:01:43 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:40:04 2008''

Revision as of 15:40, 20 March 2008

Image:2jch.jpg


PDB ID 2jch

Drag the structure with the mouse to rotate
, resolution 2.40Å
Sites: , , and
Ligands: , , and
Coordinates: save as pdb, mmCIF, xml



STRUCTURAL AND MECHANISTIC BASIS OF PENICILLIN BINDING PROTEIN INHIBITION BY LACTIVICINS


Overview

Beta-lactam antibiotics, including penicillins and cephalosporins, inhibit penicillin-binding proteins (PBPs), which are essential for bacterial cell wall biogenesis. Pathogenic bacteria have evolved efficient antibiotic resistance mechanisms that, in Gram-positive bacteria, include mutations to PBPs that enable them to avoid beta-lactam inhibition. Lactivicin (LTV; 1) contains separate cycloserine and gamma-lactone rings and is the only known natural PBP inhibitor that does not contain a beta-lactam. Here we show that LTV and a more potent analog, phenoxyacetyl-LTV (PLTV; 2), are active against clinically isolated, penicillin-resistant Streptococcus pneumoniae strains. Crystallographic analyses of S. pneumoniae PBP1b reveal that LTV and PLTV inhibition involves opening of both monocyclic cycloserine and gamma-lactone rings. In PBP1b complexes, the ring-derived atoms from LTV and PLTV show a notable structural convergence with those derived from a complexed cephalosporin (cefotaxime; 3). The structures imply that derivatives of LTV will be useful in the search for new antibiotics with activity against beta-lactam-resistant bacteria.

About this Structure

2JCH is a Single protein structure of sequence from Streptococcus pneumoniae r6. Full crystallographic information is available from OCA.

Reference

Structural and mechanistic basis of penicillin-binding protein inhibition by lactivicins., Macheboeuf P, Fischer DS, Brown T Jr, Zervosen A, Luxen A, Joris B, Dessen A, Schofield CJ, Nat Chem Biol. 2007 Sep;3(9):565-9. Epub 2007 Aug 5. PMID:17676039

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