1qwy
From Proteopedia
(New page: 200px<br /><applet load="1qwy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qwy, resolution 1.30Å" /> '''Latent LytM at 1.3 A...) |
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| - | [[Image:1qwy.jpg|left|200px]]<br /><applet load="1qwy" size=" | + | [[Image:1qwy.jpg|left|200px]]<br /><applet load="1qwy" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1qwy, resolution 1.30Å" /> | caption="1qwy, resolution 1.30Å" /> | ||
'''Latent LytM at 1.3 A resolution'''<br /> | '''Latent LytM at 1.3 A resolution'''<br /> | ||
==Overview== | ==Overview== | ||
| - | LytM, an autolysin from Staphylococcus aureus, is a Zn(2+)-dependent | + | 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== | ==About this Structure== | ||
| - | 1QWY 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 ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1QWY 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> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QWY OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bochtler, M.]] | [[Category: Bochtler, M.]] | ||
[[Category: Marcyjaniak, M.]] | [[Category: Marcyjaniak, M.]] | ||
| - | [[Category: Odintsov, S | + | [[Category: Odintsov, S G.]] |
[[Category: Sabala, I.]] | [[Category: Sabala, I.]] | ||
[[Category: ZN]] | [[Category: ZN]] | ||
[[Category: lytm lysostaphin metalloprotease asparagine switch]] | [[Category: lytm lysostaphin metalloprotease asparagine switch]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:44:36 2008'' |
Revision as of 12:44, 21 February 2008
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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 with as ligand. 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 Feb 21 14:44:36 2008
