1y79

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[[Image:1y79.gif|left|200px]]
[[Image:1y79.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1y79 |SIZE=350|CAPTION= <scene name='initialview01'>1y79</scene>, resolution 2.00&Aring;
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The line below this paragraph, containing "STRUCTURE_1y79", 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=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=LYS:LYSINE'>LYS</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= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidyl-dipeptidase_Dcp Peptidyl-dipeptidase Dcp], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.15.5 3.4.15.5] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= dcp ([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_1y79| PDB=1y79 | SCENE= }}
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|RELATEDENTRY=[[1i1i|1I1I]], [[1s4b|1S4B]], [[1o86|1O86]], [[1j36|1J36]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1y79 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y79 OCA], [http://www.ebi.ac.uk/pdbsum/1y79 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1y79 RCSB]</span>
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}}
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'''Crystal Structure of the E.coli Dipeptidyl Carboxypeptidase Dcp in Complex with a Peptidic Inhibitor'''
'''Crystal Structure of the E.coli Dipeptidyl Carboxypeptidase Dcp in Complex with a Peptidic Inhibitor'''
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[[Category: Lang, R.]]
[[Category: Lang, R.]]
[[Category: Maskos, K.]]
[[Category: Maskos, K.]]
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[[Category: ace]]
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[[Category: Ace]]
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[[Category: carboxypeptidase]]
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[[Category: Carboxypeptidase]]
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[[Category: dcp]]
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[[Category: Dcp]]
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[[Category: hinge bending]]
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[[Category: Hinge bending]]
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[[Category: neurolysin]]
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[[Category: Neurolysin]]
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[[Category: peptidyl dipeptidase]]
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[[Category: Peptidyl dipeptidase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:57:13 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:59:37 2008''
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Revision as of 12:57, 3 May 2008

Template:STRUCTURE 1y79

Crystal Structure of the E.coli Dipeptidyl Carboxypeptidase Dcp in Complex with a Peptidic Inhibitor


Overview

Dcp from Escherichia coli is a 680 residue cytoplasmic peptidase, which shows a strict dipeptidyl carboxypeptidase activity. Although Dcp had been assigned to the angiotensin I-converting enzymes (ACE) due to blockage by typical ACE inhibitors, it is currently grouped into the M3 family of mono zinc peptidases, which also contains the endopeptidases neurolysin and thimet oligopeptidase (TOP). We have cloned, expressed, purified, and crystallized Dcp in the presence of an octapeptide "inhibitor", and have determined its 2.0A crystal structure using MAD methods. The analysis revealed that Dcp consists of two half shell-like subdomains, which enclose an almost closed two-chamber cavity. In this cavity, two dipeptide products presumably generated by Dcp cleavage of the octapeptide bind to the thermolysin-like active site fixed to side-chains, which are provided by both subdomains. In particular, an Arg side-chain backed by a Glu residue, together with two Tyr phenolic groups provide a charged anchor for fixing the C-terminal carboxylate group of the P2' residue of a bound substrate, explaining the strict dipeptidyl carboxypeptidase specificity of Dcp. Tetrapeptidic substrates are fixed only via their main-chain functions from P2 to P2', suggesting a broad residue specificity for Dcp. Both subdomains exhibit very similar chain folds as the equivalent but abducted subdomains of neurolysin and TOP. Therefore, this "product-bound" Dcp structure seems to represent the inhibitor/substrate-bound "closed" form of the M3 peptidases, generated from the free "open" substrate-accessible form by a hinge-bending mechanism. A similar mechanism has recently been demonstrated experimentally for ACE2.

About this Structure

1Y79 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Crystal structure of the E. coli dipeptidyl carboxypeptidase Dcp: further indication of a ligand-dependent hinge movement mechanism., Comellas-Bigler M, Lang R, Bode W, Maskos K, J Mol Biol. 2005 May 27;349(1):99-112. Epub 2005 Mar 25. PMID:15876371 Page seeded by OCA on Sat May 3 15:57:13 2008

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