2b44: Difference between revisions

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[[Image:2b44.gif|left|200px]]<br /><applet load="2b44" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:2b44.gif|left|200px]]
caption="2b44, resolution 1.83&Aring;" />
 
'''Truncated S. aureus LytM, P 32 2 1 crystal form'''<br />
{{Structure
|PDB= 2b44 |SIZE=350|CAPTION= <scene name='initialview01'>2b44</scene>, resolution 1.83&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Lysostaphin Lysostaphin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.75 3.4.24.75]
|GENE= lytM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 Staphylococcus aureus])
}}
 
'''Truncated S. aureus LytM, P 32 2 1 crystal form'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
2B44 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=PO4:'>PO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Lysostaphin Lysostaphin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.75 3.4.24.75] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B44 OCA].  
2B44 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B44 OCA].  


==Reference==
==Reference==
Crystal structures of active LytM., Firczuk M, Mucha A, Bochtler M, J Mol Biol. 2005 Dec 2;354(3):578-90. Epub 2005 Oct 18. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16269153 16269153]
Crystal structures of active LytM., Firczuk M, Mucha A, Bochtler M, J Mol Biol. 2005 Dec 2;354(3):578-90. Epub 2005 Oct 18. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16269153 16269153]
[[Category: Lysostaphin]]
[[Category: Lysostaphin]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: peptidoglycan amidase]]
[[Category: peptidoglycan amidase]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:33:57 2008''
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Revision as of 16:57, 20 March 2008

File:2b44.gif


PDB ID 2b44

Drag the structure with the mouse to rotate
, resolution 1.83Å
Ligands: and
Gene: lytM (Staphylococcus aureus)
Activity: Lysostaphin, with EC number 3.4.24.75
Coordinates: save as pdb, mmCIF, xml



Truncated S. aureus LytM, P 32 2 1 crystal form


OverviewOverview

Lysostaphin-type enzymes are metalloendopeptidases that are present in bacteriophages and in bacteria. They share the catalytic domain, but normally contain other domains as well. The well-characterized enzymes in this group are all specific for the pentaglycine crosslinks in the cell walls of some Gram-positive bacterial species. Lysostaphin-type enzymes are synthesized as secreted preproenzymes and require proteolytic activation for maturation. Although lysostaphin, the prototypical peptidase in the group, is widely used as a tool in biotechnology and developed as an antistaphylococcal agent, the detailed structure of this enzyme is unknown. So far, only one lysostaphin-type enzyme, the Staphylococcus aureus autolysin LytM, has been crystallized in its full-length, inactive form. Here, we describe the synthesis of a convenient reporter substrate, characterize the metal and pH-dependence of an active LytM fragment, and present its crystal structure in three crystal forms at different pH values that either support or do not support activity. In all structures, we find an extended, long and narrow groove that has the active site at its bottom and is delineated on the sides by the most flexible regions of the molecule. In two cases, the groove is partially filled by a loop of a neighbouring molecule in the crystal. As the loop contains three consecutive glycine residues, this crystal packing effect supports the interpretation that the groove is the substrate-binding cleft. To characterize the substrate-binding mode more closely, a phosphinate analogue of tetraglycine was synthesized. Although tetraglycine is a substrate of the active LytM fragment, the phosphinate analogue turned out to be a very poor inhibitor. Crystals that were grown in its presence contained an L+-tartrate molecule from the crystallization buffer and not the phosphinate in the active site.

About this StructureAbout this Structure

2B44 is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structures of active LytM., Firczuk M, Mucha A, Bochtler M, J Mol Biol. 2005 Dec 2;354(3):578-90. Epub 2005 Oct 18. PMID:16269153

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