1u10

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[[Image:1u10.gif|left|200px]]
[[Image:1u10.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1u10 |SIZE=350|CAPTION= <scene name='initialview01'>1u10</scene>, resolution 2.40&Aring;
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The line below this paragraph, containing "STRUCTURE_1u10", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY=
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or leave the SCENE parameter empty for the default display.
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|GENE= mepA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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|DOMAIN=
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{{STRUCTURE_1u10| PDB=1u10 | SCENE= }}
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|RELATEDENTRY=[[1tzp|1TZP]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1u10 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u10 OCA], [http://www.ebi.ac.uk/pdbsum/1u10 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1u10 RCSB]</span>
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}}
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'''MEPA, active form with ZN in P1'''
'''MEPA, active form with ZN in P1'''
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[[Category: Odintsov, S G.]]
[[Category: Odintsov, S G.]]
[[Category: Sabala, I.]]
[[Category: Sabala, I.]]
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[[Category: las enzyme]]
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[[Category: Las enzyme]]
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[[Category: metallopeptidase]]
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[[Category: Metallopeptidase]]
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[[Category: peptidoglycan hydrolase]]
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[[Category: Peptidoglycan hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:37:10 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:03:53 2008''
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Revision as of 07:37, 3 May 2008

Template:STRUCTURE 1u10

MEPA, active form with ZN in P1


Overview

LAS enzymes are a group of metallopeptidases that share an active site architecture and a core folding motif and have been named according to the group members lysostaphin, D-Ala-D-Ala carboxypeptidase and sonic hedgehog. Escherichia coli MepA is a periplasmic, penicillin-insensitive murein endopeptidase that cleaves the D-alanyl-meso-2,6-diamino-pimelyl amide bond in E. coli peptidoglycan. The enzyme lacks sequence similarity with other peptidases, and is currently classified as a peptidase of unknown fold and catalytic class in all major data bases. Here, we build on our observation that two motifs, characteristic of the newly described LAS group of metallopeptidases, are conserved in MepA-type sequences. We demonstrate that recombinant E. coli MepA is sensitive to metal chelators and that mutations in the predicted Zn2+ ligands His-113, Asp-120, and His-211 inactivate the enzyme. Moreover, we present the crystal structure of MepA. The active site of the enzyme is most similar to the active sites of lysostaphin and D-Ala-D-Ala carboxypeptidase, and the fold is most closely related to the N-domain of sonic hedgehog. We conclude that MepA-type peptidases are LAS enzymes.

About this Structure

1U10 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Peptidoglycan amidase MepA is a LAS metallopeptidase., Marcyjaniak M, Odintsov SG, Sabala I, Bochtler M, J Biol Chem. 2004 Oct 15;279(42):43982-9. Epub 2004 Jul 29. PMID:15292190 Page seeded by OCA on Sat May 3 10:37:10 2008

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