1gvm
From Proteopedia
(New page: 200px<br /> <applet load="1gvm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gvm, resolution 2.80Å" /> '''CHOLINE BINDING DOM...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1GVM is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae]] with CHT, DDQ and TRS as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.28 3.5.1.28]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GVM OCA]]. | + | 1GVM is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae]] with CHT, DDQ and TRS as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/N-acetylmuramoyl-L-alanine_amidase N-acetylmuramoyl-L-alanine amidase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.28 3.5.1.28]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GVM OCA]]. |
==Reference== | ==Reference== | ||
Two new crystal forms of the choline-binding domain of the major pneumococcal autolysin: insights into the dynamics of the active homodimer., Fernandez-Tornero C, Garcia E, Lopez R, Gimenez-Gallego G, Romero A, J Mol Biol. 2002 Aug 2;321(1):163-73. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12139941 12139941] | Two new crystal forms of the choline-binding domain of the major pneumococcal autolysin: insights into the dynamics of the active homodimer., Fernandez-Tornero C, Garcia E, Lopez R, Gimenez-Gallego G, Romero A, J Mol Biol. 2002 Aug 2;321(1):163-73. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12139941 12139941] | ||
| + | [[Category: N-acetylmuramoyl-L-alanine amidase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Streptococcus pneumoniae]] | [[Category: Streptococcus pneumoniae]] | ||
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[[Category: choline-binding domain]] | [[Category: choline-binding domain]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:27:40 2007'' |
Revision as of 11:22, 30 October 2007
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CHOLINE BINDING DOMAIN OF THE MAJOR AUTOLYSIN (C-LYTA) FROM STREPTOCOCCUS PNEUMONIAE
Overview
Very little is known about the in vivo regulation of the catalytic, activity of the major pneumococcal autolysin (LytA), a surface-exposed, enzyme that rules the self-destruction of pneumococcal cells through, degradation of their peptidoglycan backbone. Two new crystal forms of the, cell wall anchoring domain of LytA were obtained, and their structures, were solved and refined to 2.4A and 2.8A resolution. The domain is a, homodimer with a boomerang-like shape in which the tertiary structure of, each monomer is comprised by six independent beta hairpins arranged in a, superhelical fashion. Choline molecules at the hydrophobic interface of, consecutive hairpins maintain this unique structure. The C-terminal, hairpin (last 13 residues of LytA) in the solenoid is responsible for the, ... [(full description)]
About this Structure
1GVM is a [Single protein] structure of sequence from [Streptococcus pneumoniae] with CHT, DDQ and TRS as [ligands]. Active as [N-acetylmuramoyl-L-alanine amidase], with EC number [3.5.1.28]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Two new crystal forms of the choline-binding domain of the major pneumococcal autolysin: insights into the dynamics of the active homodimer., Fernandez-Tornero C, Garcia E, Lopez R, Gimenez-Gallego G, Romero A, J Mol Biol. 2002 Aug 2;321(1):163-73. PMID:12139941
Page seeded by OCA on Tue Oct 30 13:27:40 2007
