1lok
From Proteopedia
(New page: 200px<br /><applet load="1lok" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lok, resolution 1.20Å" /> '''The 1.20 Angstrom Re...) |
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| - | [[Image:1lok.jpg|left|200px]]<br /><applet load="1lok" size=" | + | [[Image:1lok.jpg|left|200px]]<br /><applet load="1lok" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1lok, resolution 1.20Å" /> | caption="1lok, resolution 1.20Å" /> | ||
'''The 1.20 Angstrom Resolution Crystal Structure of the Aminopeptidase from Aeromonas proteolytica Complexed with Tris: A Tale of Buffer Inhibition'''<br /> | '''The 1.20 Angstrom Resolution Crystal Structure of the Aminopeptidase from Aeromonas proteolytica Complexed with Tris: A Tale of Buffer Inhibition'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The aminopeptidase from Aeromonas proteolytica (AAP) is a bridged | + | 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== | ==About this Structure== | ||
| - | 1LOK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vibrio_proteolyticus Vibrio proteolyticus] with ZN, NA, SCN and TRS as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | + | 1LOK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vibrio_proteolyticus Vibrio proteolyticus] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=SCN:'>SCN</scene> and <scene name='pdbligand=TRS:'>TRS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LOK OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Vibrio proteolyticus]] | [[Category: Vibrio proteolyticus]] | ||
| - | [[Category: Bienvenue, D | + | [[Category: Bienvenue, D L.]] |
| - | [[Category: Bzymek, K | + | [[Category: Bzymek, K P.]] |
| - | [[Category: Desmarais, W | + | [[Category: Desmarais, W T.]] |
| - | [[Category: Holz, R | + | [[Category: Holz, R C.]] |
| - | [[Category: Petsko, G | + | [[Category: Petsko, G A.]] |
[[Category: Ringe, D.]] | [[Category: Ringe, D.]] | ||
[[Category: NA]] | [[Category: NA]] | ||
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[[Category: tris]] | [[Category: tris]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:46:58 2008'' |
Revision as of 11:47, 21 February 2008
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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
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 with , , and as ligands. Active as Bacterial leucyl aminopeptidase, with EC number 3.4.11.10 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
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