1lok
From Proteopedia
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| - | [[Image:1lok.jpg|left|200px]] | + | [[Image:1lok.jpg|left|200px]] |
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| - | '''The 1.20 Angstrom Resolution Crystal Structure of the Aminopeptidase from Aeromonas proteolytica Complexed with Tris: A Tale of Buffer Inhibition''' | + | {{Structure |
| + | |PDB= 1lok |SIZE=350|CAPTION= <scene name='initialview01'>1lok</scene>, resolution 1.20Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SCN:THIOCYANATE+ION'>SCN</scene> and <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Bacterial_leucyl_aminopeptidase Bacterial leucyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.10 3.4.11.10] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''The 1.20 Angstrom Resolution Crystal Structure of the Aminopeptidase from Aeromonas proteolytica Complexed with Tris: A Tale of Buffer Inhibition''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1LOK is a [ | + | 1LOK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Vibrio_proteolyticus Vibrio proteolyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LOK OCA]. |
==Reference== | ==Reference== | ||
| - | The 1.20 A resolution crystal structure of the aminopeptidase from Aeromonas proteolytica complexed with tris: a tale of buffer inhibition., Desmarais WT, Bienvenue DL, Bzymek KP, Holz RC, Petsko GA, Ringe D, Structure. 2002 Aug;10(8):1063-72. PMID:[http:// | + | The 1.20 A resolution crystal structure of the aminopeptidase from Aeromonas proteolytica complexed with tris: a tale of buffer inhibition., Desmarais WT, Bienvenue DL, Bzymek KP, Holz RC, Petsko GA, Ringe D, Structure. 2002 Aug;10(8):1063-72. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12176384 12176384] |
[[Category: Bacterial leucyl aminopeptidase]] | [[Category: Bacterial leucyl aminopeptidase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: metal coordination]] | [[Category: metal coordination]] | ||
[[Category: metalloenzyme]] | [[Category: metalloenzyme]] | ||
| - | [[Category: | + | [[Category: tri]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:33:18 2008'' |
Revision as of 10:33, 20 March 2008
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| , resolution 1.20Å | |||||||
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| Ligands: | , , and | ||||||
| Activity: | Bacterial leucyl aminopeptidase, with EC number 3.4.11.10 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
The 1.20 Angstrom Resolution Crystal Structure of the Aminopeptidase from Aeromonas proteolytica Complexed with Tris: A Tale of Buffer Inhibition
Overview
The aminopeptidase from Aeromonas proteolytica (AAP) is a bridged bimetallic enzyme that removes the N-terminal amino acid from a peptide chain. To fully understand the metal roles in the reaction pathway of AAP we have solved the 1.20 A resolution crystal structure of native AAP (PDB ID = 1LOK). The high-quality electron density maps showed a single Tris molecule chelated to the active site Zn(2+), alternate side chain conformations for some side chains, a sodium ion that mediates a crystal contact, a surface thiocyanate ion, and several potential hydrogen atoms. In addition, the high precision of the atomic positions has led to insight into the protonation states of some of the active site amino acid side chains.
About this Structure
1LOK is a Single protein structure of sequence from Vibrio proteolyticus. Full crystallographic information is available from OCA.
Reference
The 1.20 A resolution crystal structure of the aminopeptidase from Aeromonas proteolytica complexed with tris: a tale of buffer inhibition., Desmarais WT, Bienvenue DL, Bzymek KP, Holz RC, Petsko GA, Ringe D, Structure. 2002 Aug;10(8):1063-72. PMID:12176384
Page seeded by OCA on Thu Mar 20 12:33:18 2008
