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2vo9
From Proteopedia
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[[Image:2vo9.png|left|200px]] | [[Image:2vo9.png|left|200px]] | ||
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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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| + | The line below this paragraph, {{ABSTRACT_PUBMED_18560152}}, adds the Publication Abstract to the page | ||
| + | (as it appears on PubMed at http://www.pubmed.gov), where 18560152 is the PubMed ID number. | ||
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| + | {{ABSTRACT_PUBMED_18560152}} | ||
==About this Structure== | ==About this Structure== | ||
| - | + | [[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== | ||
| + | <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
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
