1h09

<table><tr><td colspan='2'>[[1h09]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bpcp1 Bpcp1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H09 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H09 FirstGlance]. <br>

</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span></td></tr>

[[https://www.uniprot.org/uniprot/LYS_BPCP1 LYS_BPCP1]] Responsible for the separation of the host daughter cells at the end of cell division and participates in the liberation of progeny bacteriophage into the medium. Strictly depends on the presence of choline-containing cell walls for activity.

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== Publication Abstract from PubMed ==

Pneumococcal bacteriophage-encoded lysins are modular choline binding proteins that have been shown to act as enzymatic antimicrobial agents (enzybiotics) against streptococcal infections. Here we present the crystal structures of the free and choline bound states of the Cpl-1 lysin, encoded by the pneumococcal phage Cp-1. While the catalytic module displays an irregular (beta/alpha)(5)beta(3) barrel, the cell wall-anchoring module is formed by six similar choline binding repeats (ChBrs), arranged into two different structural regions: a left-handed superhelical domain configuring two choline binding sites, and a beta sheet domain that contributes in bringing together the whole structure. Crystallographic and site-directed mutagenesis studies allow us to propose a general catalytic mechanism for the whole glycoside hydrolase family 25. Our work provides the first complete structure of a member of the large family of choline binding proteins and reveals that ChBrs are versatile elements able to tune the evolution and specificity of the pneumococcal surface proteins.

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:14527392<ref>PMID:14527392</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1h09" style="background-color:#fffaf0;"></div>

*[[Lysin|Lysin]]

== References ==

<references/>

[[Category: Bpcp1]]

[[Category: Lysozyme]]

[[Category: Albert, A]]

[[Category: Garcia, J L]]

[[Category: Garcia, P]]

[[Category: Hermoso, J A]]

[[Category: Martinez-Ripoll, M]]

[[Category: Menendez, M]]

[[Category: Monterroso, B]]

[[Category: Pneumococcal cell wall degradation]]