2j8f: Difference between revisions

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~~'''~~CRYSTAL STRUCTURE OF THE MODULAR CPL-1 ENDOLYSIN COMPLEXED WITH A PEPTIDOGLYCAN ANALOGUE (E94Q MUTANT IN COMPLEX WITH A DISACCHARIDE-PENTAPEPTIDE)~~'''~~

===CRYSTAL STRUCTURE OF THE MODULAR CPL-1 ENDOLYSIN COMPLEXED WITH A PEPTIDOGLYCAN ANALOGUE (E94Q MUTANT IN COMPLEX WITH A DISACCHARIDE-PENTAPEPTIDE)===

~~==Overview==~~

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~~Pneumococcal bacteriophage~~-~~encoded lysins are modular proteins that have been shown to act as enzymatic antimicrobial agents (enzybiotics) in treatment of streptococcal infections. The first x~~-~~ray crystal structures of the Cpl-1 lysin, encoded by the pneumococcal phage Cp-1, in complex with three bacterial cell wall peptidoglycan (PG) analogues are reported herein.~~ The ~~Cpl-1 structure is folded in two well defined modules, one responsible for anchoring to the pneumococcal cell wall and the other~~, ~~a catalytic module~~, ~~that hydrolyzes~~ the ~~PG. Conformational rearrangement of Tyr-127 is a critical event in molecular recognition of a stretch of five saccharide rings of~~ the ~~polymeric peptidoglycan~~ (~~cell wall). The PG is bound~~ at ~~a stretch of the surface that is defined as the peptidoglycan-binding sites 1 and 2, the juncture of which catalysis takes place~~. ~~The peptidoglycan-binding site 1 binds to a stretch of three saccharides of the peptidoglycan in a conformation essentially identical to that of the peptidoglycan in solution~~. ~~In contrast~~, ~~binding of two peptidoglycan saccharides at~~ the ~~peptidoglycan~~-binding site 2 introduces a kink into the solution structure of the peptidoglycan, en route to catalytic turnover. These findings provide the first structural evidence on recognition of the peptidoglycan and shed light on the discrete events of cell wall degradation by Cpl-1.

The line below this paragraph, {{ABSTRACT_PUBMED_17581815}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 17581815 is the PubMed ID number.

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==About this Structure==

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==Reference==

Elucidation of the molecular recognition of bacterial cell wall by modular pneumococcal phage endolysin CPL-1., Perez-Dorado I, Campillo NE, Monterroso B, Hesek D, Lee M, Paez JA, Garcia P, Martinez-Ripoll M, Garcia JL, Mobashery S, Menendez M, Hermoso JA, J Biol Chem. 2007 Aug 24;282(34):24990-9. Epub 2007 Jun 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17581815 17581815]

Structural basis for selective recognition of pneumococcal cell wall by modular endolysin from phage Cp-1., Hermoso JA, Monterroso B, Albert A, Galan B, Ahrazem O, Garcia P, Martinez-Ripoll M, Garcia JL, Menendez M, Structure. 2003 Oct;11(10):1239-49. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14527392 14527392]

Crystallization and preliminary X-ray diffraction studies of the complete modular endolysin from Cp-1, a phage infecting Streptococcus pneumoniae., Monterroso B, Albert A, Martinez-Ripoll M, Garcia P, Garcia JL, Menendez M, Hermoso JA, Acta Crystallogr D Biol Crystallogr. 2002 Sep;58(Pt 9):1487-9. Epub 2002, Aug 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12198311 12198311]

[[Category: Bacteriophage cp-1]]

[[Category: Lysozyme]]

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[[Category: Multimodular]]

[[Category: Pneumococcal cell wall degradation]]

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-[[Image:2j8f.jpg|left|200px]]
+{{Seed}}
+[[Image:2j8f.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2j8f|  PDB=2j8f  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF THE MODULAR CPL-1 ENDOLYSIN COMPLEXED WITH A PEPTIDOGLYCAN ANALOGUE (E94Q MUTANT IN COMPLEX WITH A DISACCHARIDE-PENTAPEPTIDE)'''
+===CRYSTAL STRUCTURE OF THE MODULAR CPL-1 ENDOLYSIN COMPLEXED WITH A PEPTIDOGLYCAN ANALOGUE (E94Q MUTANT IN COMPLEX WITH A DISACCHARIDE-PENTAPEPTIDE)===
-==Overview==
+<!--
-Pneumococcal bacteriophage-encoded lysins are modular proteins that have been shown to act as enzymatic antimicrobial agents (enzybiotics) in treatment of streptococcal infections. The first x-ray crystal structures of the Cpl-1 lysin, encoded by the pneumococcal phage Cp-1, in complex with three bacterial cell wall peptidoglycan (PG) analogues are reported herein. The Cpl-1 structure is folded in two well defined modules, one responsible for anchoring to the pneumococcal cell wall and the other, a catalytic module, that hydrolyzes the PG. Conformational rearrangement of Tyr-127 is a critical event in molecular recognition of a stretch of five saccharide rings of the polymeric peptidoglycan (cell wall). The PG is bound at a stretch of the surface that is defined as the peptidoglycan-binding sites 1 and 2, the juncture of which catalysis takes place. The peptidoglycan-binding site 1 binds to a stretch of three saccharides of the peptidoglycan in a conformation essentially identical to that of the peptidoglycan in solution. In contrast, binding of two peptidoglycan saccharides at the peptidoglycan-binding site 2 introduces a kink into the solution structure of the peptidoglycan, en route to catalytic turnover. These findings provide the first structural evidence on recognition of the peptidoglycan and shed light on the discrete events of cell wall degradation by Cpl-1.
+The line below this paragraph, {{ABSTRACT_PUBMED_17581815}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17581815 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17581815}}
 ==About this Structure==
@@ Line 20: / Line 24: @@
 ==Reference==
 Elucidation of the molecular recognition of bacterial cell wall by modular pneumococcal phage endolysin CPL-1., Perez-Dorado I, Campillo NE, Monterroso B, Hesek D, Lee M, Paez JA, Garcia P, Martinez-Ripoll M, Garcia JL, Mobashery S, Menendez M, Hermoso JA, J Biol Chem. 2007 Aug 24;282(34):24990-9. Epub 2007 Jun 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17581815 17581815]
+Structural basis for selective recognition of pneumococcal cell wall by modular endolysin from phage Cp-1., Hermoso JA, Monterroso B, Albert A, Galan B, Ahrazem O, Garcia P, Martinez-Ripoll M, Garcia JL, Menendez M, Structure. 2003 Oct;11(10):1239-49. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14527392 14527392]
+Crystallization and preliminary X-ray diffraction studies of the complete modular endolysin from Cp-1, a phage infecting Streptococcus pneumoniae., Monterroso B, Albert A, Martinez-Ripoll M, Garcia P, Garcia JL, Menendez M, Hermoso JA, Acta Crystallogr D Biol Crystallogr. 2002 Sep;58(Pt 9):1487-9. Epub 2002, Aug 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12198311 12198311]
 [[Category: Bacteriophage cp-1]]
 [[Category: Lysozyme]]
@@ Line 33: / Line 41: @@
 [[Category: Multimodular]]
 [[Category: Pneumococcal cell wall degradation]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 08:30:05 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:20:47 2008''