1tzp
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1tzp |SIZE=350|CAPTION= <scene name='initialview01'>1tzp</scene>, resolution 1.40Å | |PDB= 1tzp |SIZE=350|CAPTION= <scene name='initialview01'>1tzp</scene>, resolution 1.40Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=BU1:1,4-BUTANEDIOL'>BU1</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= mepA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= mepA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1u10|1U10]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tzp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tzp OCA], [http://www.ebi.ac.uk/pdbsum/1tzp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tzp RCSB]</span> | ||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: Odintsov, S G.]] | [[Category: Odintsov, S G.]] | ||
[[Category: Sabala, I.]] | [[Category: Sabala, I.]] | ||
| - | [[Category: BU1]] | ||
| - | [[Category: SO4]] | ||
[[Category: las enzyme]] | [[Category: las enzyme]] | ||
[[Category: metallopeptidase]] | [[Category: metallopeptidase]] | ||
[[Category: peptidoglycan hydrolase]] | [[Category: peptidoglycan hydrolase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:03:20 2008'' |
Revision as of 21:03, 30 March 2008
| |||||||
| , resolution 1.40Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | mepA (Escherichia coli) | ||||||
| Related: | 1U10
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
MEPA, inactive form without ZN in P21
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
1TZP 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 Mon Mar 31 00:03:20 2008
