1hcx
From Proteopedia
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| - | [[Image:1hcx.gif|left|200px]]<br /> | + | [[Image:1hcx.gif|left|200px]]<br /><applet load="1hcx" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1hcx" size=" | + | |
caption="1hcx, resolution 2.60Å" /> | caption="1hcx, resolution 2.60Å" /> | ||
'''CHOLINE BINDING DOMAIN OF THE MAJOR AUTOLYSIN (C-LYTA) FROM STREPTOCOCCUS PNEUMONIAE'''<br /> | '''CHOLINE BINDING DOMAIN OF THE MAJOR AUTOLYSIN (C-LYTA) FROM STREPTOCOCCUS PNEUMONIAE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1HCX 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 TPT, CHT and DDQ 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] | + | 1HCX 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 <scene name='pdbligand=TPT:'>TPT</scene>, <scene name='pdbligand=CHT:'>CHT</scene> and <scene name='pdbligand=DDQ:'>DDQ</scene> 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] Known structural/functional Site: <scene name='pdbsite=1:Tpt+Binding+Site+For+Chain+A'>1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HCX OCA]. |
==Reference== | ==Reference== | ||
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[[Category: choline-binding domain]] | [[Category: choline-binding domain]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:48:34 2008'' |
Revision as of 07:48, 3 February 2008
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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 with , and as ligands. Active as N-acetylmuramoyl-L-alanine amidase, with EC number 3.5.1.28 Known structural/functional Site: . 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
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