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1qwy
From Proteopedia
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| - | [[Image:1qwy.jpg|left|200px]] | + | [[Image:1qwy.jpg|left|200px]] |
| - | + | ||
| - | '''Latent LytM at 1.3 A resolution''' | + | {{Structure |
| + | |PDB= 1qwy |SIZE=350|CAPTION= <scene name='initialview01'>1qwy</scene>, resolution 1.30Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= LytM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 Staphylococcus aureus]) | ||
| + | }} | ||
| + | |||
| + | '''Latent LytM at 1.3 A resolution''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1QWY is a [ | + | 1QWY 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=1QWY OCA]. |
==Reference== | ==Reference== | ||
| - | Latent LytM at 1.3A resolution., Odintsov SG, Sabala I, Marcyjaniak M, Bochtler M, J Mol Biol. 2004 Jan 16;335(3):775-85. PMID:[http:// | + | Latent LytM at 1.3A resolution., Odintsov SG, Sabala I, Marcyjaniak M, Bochtler M, J Mol Biol. 2004 Jan 16;335(3):775-85. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14687573 14687573] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Staphylococcus aureus]] | [[Category: Staphylococcus aureus]] | ||
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[[Category: lytm lysostaphin metalloprotease asparagine switch]] | [[Category: lytm lysostaphin metalloprotease asparagine switch]] | ||
| - | ''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 13:43:49 2008'' |
Revision as of 11:43, 20 March 2008
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| , resolution 1.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | LytM (Staphylococcus aureus) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Latent LytM at 1.3 A resolution
Overview
LytM, an autolysin from Staphylococcus aureus, is a Zn(2+)-dependent glycyl-glycine endopeptidase with a characteristic HxH motif that belongs to the lysostaphin-type (MEROPS M23/37) of metallopeptidases. Here, we present the 1.3A crystal structure of LytM, the first structure of a lysostaphin-type peptidase. In the LytM structure, the Zn(2+) is tetrahedrally coordinated by the side-chains of N117, H210, D214 and H293, the second histidine of the HxH motif. Although close to the active-site, H291, the first histidine of the HxH motif, is not directly involved in Zn(2+)-coordination, and there is no water molecule in the coordination sphere of the Zn(2+), suggesting that the crystal structure shows a latent form of the enzyme. Although LytM has not previously been considered as a proenzyme, we show that a truncated version of LytM that lacks the N-terminal part with the poorly conserved Zn(2+) ligand N117 has much higher specific activity than full-length enzyme. This observation is consistent with the known removal of profragments in other lysostaphin-type proteins and with a prior observation of an active LytM degradation fragment in S.aureus supernatant. The "asparagine switch" in LytM is analogous to the "cysteine switch" in pro-matrix metalloproteases.
About this Structure
1QWY is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.
Reference
Latent LytM at 1.3A resolution., Odintsov SG, Sabala I, Marcyjaniak M, Bochtler M, J Mol Biol. 2004 Jan 16;335(3):775-85. PMID:14687573
Page seeded by OCA on Thu Mar 20 13:43:49 2008
