1itu
From Proteopedia
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|PDB= 1itu |SIZE=350|CAPTION= <scene name='initialview01'>1itu</scene>, resolution 2.00Å | |PDB= 1itu |SIZE=350|CAPTION= <scene name='initialview01'>1itu</scene>, resolution 2.00Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> | + | |LIGAND= <scene name='pdbligand=CIL:CILASTATIN'>CIL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
| - | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Membrane_dipeptidase Membrane dipeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.13.19 3.4.13.19] </span> | |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1itq|1ITQ]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1itu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1itu OCA], [http://www.ebi.ac.uk/pdbsum/1itu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1itu RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==Overview== | ||
Human renal dipeptidase is a membrane-bound glycoprotein hydrolyzing dipeptides and is involved in hydrolytic metabolism of penem and carbapenem beta-lactam antibiotics. The crystal structures of the saccharide-trimmed enzyme are determined as unliganded and inhibitor-liganded forms. They are informative for designing new antibiotics that are not hydrolyzed by this enzyme. The active site in each of the (alpha/beta)(8) barrel subunits of the homodimeric molecule is composed of binuclear zinc ions bridged by the Glu125 side-chain located at the bottom of the barrel, and it faces toward the microvillar membrane of a kidney tubule. A dipeptidyl moiety of the therapeutically used cilastatin inhibitor is fully accommodated in the active-site pocket, which is small enough for precise recognition of dipeptide substrates. The barrel and active-site architectures utilizing catalytic metal ions exhibit unexpected similarities to those of the murine adenosine deaminase and the catalytic domain of the bacterial urease. | Human renal dipeptidase is a membrane-bound glycoprotein hydrolyzing dipeptides and is involved in hydrolytic metabolism of penem and carbapenem beta-lactam antibiotics. The crystal structures of the saccharide-trimmed enzyme are determined as unliganded and inhibitor-liganded forms. They are informative for designing new antibiotics that are not hydrolyzed by this enzyme. The active site in each of the (alpha/beta)(8) barrel subunits of the homodimeric molecule is composed of binuclear zinc ions bridged by the Glu125 side-chain located at the bottom of the barrel, and it faces toward the microvillar membrane of a kidney tubule. A dipeptidyl moiety of the therapeutically used cilastatin inhibitor is fully accommodated in the active-site pocket, which is small enough for precise recognition of dipeptide substrates. The barrel and active-site architectures utilizing catalytic metal ions exhibit unexpected similarities to those of the murine adenosine deaminase and the catalytic domain of the bacterial urease. | ||
| - | |||
| - | ==Disease== | ||
| - | Known disease associated with this structure: Dystonia-12 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=182350 182350]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Satow, Y.]] | [[Category: Satow, Y.]] | ||
[[Category: Tsujimoto, M.]] | [[Category: Tsujimoto, M.]] | ||
| - | [[Category: CIL]] | ||
| - | [[Category: NAG]] | ||
| - | [[Category: ZN]] | ||
[[Category: cilastatin]] | [[Category: cilastatin]] | ||
[[Category: complex (hydrolase/inhibitor)]] | [[Category: complex (hydrolase/inhibitor)]] | ||
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[[Category: zinc protease beta-lactamase]] | [[Category: zinc protease beta-lactamase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:24:34 2008'' |
Revision as of 18:24, 30 March 2008
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| , resolution 2.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Activity: | Membrane dipeptidase, with EC number 3.4.13.19 | ||||||
| Related: | 1ITQ
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HUMAN RENAL DIPEPTIDASE COMPLEXED WITH CILASTATIN
Overview
Human renal dipeptidase is a membrane-bound glycoprotein hydrolyzing dipeptides and is involved in hydrolytic metabolism of penem and carbapenem beta-lactam antibiotics. The crystal structures of the saccharide-trimmed enzyme are determined as unliganded and inhibitor-liganded forms. They are informative for designing new antibiotics that are not hydrolyzed by this enzyme. The active site in each of the (alpha/beta)(8) barrel subunits of the homodimeric molecule is composed of binuclear zinc ions bridged by the Glu125 side-chain located at the bottom of the barrel, and it faces toward the microvillar membrane of a kidney tubule. A dipeptidyl moiety of the therapeutically used cilastatin inhibitor is fully accommodated in the active-site pocket, which is small enough for precise recognition of dipeptide substrates. The barrel and active-site architectures utilizing catalytic metal ions exhibit unexpected similarities to those of the murine adenosine deaminase and the catalytic domain of the bacterial urease.
About this Structure
1ITU is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of human renal dipeptidase involved in beta-lactam hydrolysis., Nitanai Y, Satow Y, Adachi H, Tsujimoto M, J Mol Biol. 2002 Aug 9;321(2):177-84. PMID:12144777
Page seeded by OCA on Sun Mar 30 21:24:34 2008
