2vo9

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===CRYSTAL STRUCTURE OF THE ENZYMATICALLY ACTIVE DOMAIN OF THE LISTERIA MONOCYTOGENES BACTERIOPHAGE 500 ENDOLYSIN PLY500===
===CRYSTAL STRUCTURE OF THE ENZYMATICALLY ACTIVE DOMAIN OF THE LISTERIA MONOCYTOGENES BACTERIOPHAGE 500 ENDOLYSIN PLY500===
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{{ABSTRACT_PUBMED_18560152}}
==About this Structure==
==About this Structure==
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2VO9 is a 3 chains structure of sequences from [http://en.wikipedia.org/wiki/Listeria_phage_a500 Listeria phage a500]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1xp2 1xp2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VO9 OCA].
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[[2vo9]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Listeria_phage_a500 Listeria phage a500]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1xp2 1xp2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VO9 OCA].
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==Reference==
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<ref group="xtra">PMID:018560152</ref><references group="xtra"/>
[[Category: Listeria phage a500]]
[[Category: Listeria phage a500]]
[[Category: Kanitz, A.]]
[[Category: Kanitz, A.]]
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[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Secreted]]
[[Category: Secreted]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 18:43:20 2009''
 

Revision as of 05:11, 10 August 2011

Image:2vo9.png

Template:STRUCTURE 2vo9

CRYSTAL STRUCTURE OF THE ENZYMATICALLY ACTIVE DOMAIN OF THE LISTERIA MONOCYTOGENES BACTERIOPHAGE 500 ENDOLYSIN PLY500

Template:ABSTRACT PUBMED 18560152

About this Structure

2vo9 is a 3 chain structure with sequence from Listeria phage a500. This structure supersedes the now removed PDB entry 1xp2. Full crystallographic information is available from OCA.

Reference

  • Korndorfer IP, Kanitz A, Danzer J, Zimmer M, Loessner MJ, Skerra A. Structural analysis of the L-alanoyl-D-glutamate endopeptidase domain of Listeria bacteriophage endolysin Ply500 reveals a new member of the LAS peptidase family. Acta Crystallogr D Biol Crystallogr. 2008 Jun;64(Pt 6):644-50. Epub 2008, May 14. PMID:18560152 doi:10.1107/S0907444908007890

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