1qwy

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{{STRUCTURE_1qwy| PDB=1qwy | SCENE= }}
{{STRUCTURE_1qwy| PDB=1qwy | SCENE= }}
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'''Latent LytM at 1.3 A resolution'''
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===Latent LytM at 1.3 A resolution===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_14687573}}
==About this Structure==
==About this Structure==
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[[Category: Sabala, I.]]
[[Category: Sabala, I.]]
[[Category: Lytm lysostaphin metalloprotease asparagine switch]]
[[Category: Lytm lysostaphin metalloprotease asparagine switch]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 16:11:12 2008''

Revision as of 13:11, 28 July 2008

Image:1qwy.png

Template:STRUCTURE 1qwy

Latent LytM at 1.3 A resolution

Template:ABSTRACT PUBMED 14687573

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

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