1h8g
From Proteopedia
(New page: 200px<br /><applet load="1h8g" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h8g, resolution 2.40Å" /> '''C-TERMINAL DOMAIN OF...) |
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| - | [[Image:1h8g.jpg|left|200px]]<br /><applet load="1h8g" size=" | + | [[Image:1h8g.jpg|left|200px]]<br /><applet load="1h8g" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1h8g, resolution 2.40Å" /> | caption="1h8g, resolution 2.40Å" /> | ||
'''C-TERMINAL DOMAIN OF THE MAJOR AUTOLYSIN (C-LYTA) FROM STREPTOCOCCUS PNEUMONIAE'''<br /> | '''C-TERMINAL DOMAIN OF THE MAJOR AUTOLYSIN (C-LYTA) FROM STREPTOCOCCUS PNEUMONIAE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Choline binding proteins are virulence determinants present in several | + | 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== | ==About this Structure== | ||
| - | 1H8G 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 as [http://en.wikipedia.org/wiki/ligand ligand]. 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] Full crystallographic information is available from [http:// | + | 1H8G 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=CHT:'>CHT</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H8G 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 Thu Feb 21 12:58:36 2008'' |
Revision as of 10:58, 21 February 2008
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C-TERMINAL 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
1H8G is a Single protein structure of sequence from Streptococcus pneumoniae with as ligand. Active as N-acetylmuramoyl-L-alanine amidase, with EC number 3.5.1.28 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 Feb 21 12:58:36 2008
