1hcx
From Proteopedia
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| - | [[Image:1hcx.gif|left|200px]] | + | [[Image:1hcx.gif|left|200px]] |
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| - | '''CHOLINE BINDING DOMAIN OF THE MAJOR AUTOLYSIN (C-LYTA) FROM STREPTOCOCCUS PNEUMONIAE''' | + | {{Structure |
| + | |PDB= 1hcx |SIZE=350|CAPTION= <scene name='initialview01'>1hcx</scene>, resolution 2.60Å | ||
| + | |SITE= <scene name='pdbsite=1:Tpt+Binding+Site+For+Chain+A'>1</scene> | ||
| + | |LIGAND= <scene name='pdbligand=TPT:2,2':6',2''-TERPYRIDINE+PLATINUM(II)'>TPT</scene>, <scene name='pdbligand=CHT:CHOLINE+ION'>CHT</scene> and <scene name='pdbligand=DDQ:DECYLAMINE-N,N-DIMETHYL-N-OXIDE'>DDQ</scene> | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= LYTA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1313 Streptococcus pneumoniae]) | ||
| + | }} | ||
| + | |||
| + | '''CHOLINE BINDING DOMAIN OF THE MAJOR AUTOLYSIN (C-LYTA) FROM STREPTOCOCCUS PNEUMONIAE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1HCX is a [ | + | 1HCX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HCX OCA]. |
==Reference== | ==Reference== | ||
| - | A novel solenoid fold in the cell wall anchoring domain of the pneumococcal virulence factor LytA., Fernandez-Tornero C, Lopez R, Garcia E, Gimenez-Gallego G, Romero A, Nat Struct Biol. 2001 Dec;8(12):1020-4. PMID:[http:// | + | A novel solenoid fold in the cell wall anchoring domain of the pneumococcal virulence factor LytA., Fernandez-Tornero C, Lopez R, Garcia E, Gimenez-Gallego G, Romero A, Nat Struct Biol. 2001 Dec;8(12):1020-4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11694890 11694890] |
[[Category: N-acetylmuramoyl-L-alanine amidase]] | [[Category: N-acetylmuramoyl-L-alanine amidase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: choline-binding domain]] | [[Category: choline-binding domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:35:34 2008'' |
Revision as of 09:35, 20 March 2008
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| , resolution 2.60Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , and | ||||||
| Gene: | LYTA (Streptococcus pneumoniae) | ||||||
| Activity: | N-acetylmuramoyl-L-alanine amidase, with EC number 3.5.1.28 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CHOLINE BINDING DOMAIN OF THE MAJOR AUTOLYSIN (C-LYTA) FROM STREPTOCOCCUS PNEUMONIAE
Overview
Choline binding proteins are virulence determinants present in several Gram-positive bacteria. Because anchorage of these proteins to the cell wall through their choline binding domain is essential for bacterial virulence, their release from the cell surface is considered a powerful target for a weapon against these pathogens. The first crystal structure of a choline binding domain, from the toxin-releasing enzyme pneumococcal major autolysin (LytA), reveals a novel solenoid fold consisting exclusively of beta-hairpins that stack to form a left-handed superhelix. This unique structure is maintained by choline molecules at the hydrophobic interface of consecutive hairpins and may be present in other choline binding proteins that share high homology to the repeated motif of the domain.
About this Structure
1HCX is a Single protein structure of sequence from Streptococcus pneumoniae. Full crystallographic information is available from OCA.
Reference
A novel solenoid fold in the cell wall anchoring domain of the pneumococcal virulence factor LytA., Fernandez-Tornero C, Lopez R, Garcia E, Gimenez-Gallego G, Romero A, Nat Struct Biol. 2001 Dec;8(12):1020-4. PMID:11694890
Page seeded by OCA on Thu Mar 20 11:35:34 2008
