2dq6: Difference between revisions

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[[Image:2dq6.gif|left|200px]]<br /><applet load="2dq6" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:2dq6.gif|left|200px]]
caption="2dq6, resolution 1.50&Aring;" />
 
'''Crystal Structure of Aminopeptidase N from Escherichia coli'''<br />
{{Structure
|PDB= 2dq6 |SIZE=350|CAPTION= <scene name='initialview01'>2dq6</scene>, resolution 1.50&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Membrane_alanyl_aminopeptidase Membrane alanyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.2 3.4.11.2]
|GENE= pepN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
}}
 
'''Crystal Structure of Aminopeptidase N from Escherichia coli'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
2DQ6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Membrane_alanyl_aminopeptidase Membrane alanyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.2 3.4.11.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DQ6 OCA].  
2DQ6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DQ6 OCA].  


==Reference==
==Reference==
Crystal structure of aminopeptidase N (proteobacteria alanyl aminopeptidase) from Escherichia coli and conformational change of methionine 260 involved in substrate recognition., Ito K, Nakajima Y, Onohara Y, Takeo M, Nakashima K, Matsubara F, Ito T, Yoshimoto T, J Biol Chem. 2006 Nov 3;281(44):33664-76. Epub 2006 Aug 2. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16885166 16885166]
Crystal structure of aminopeptidase N (proteobacteria alanyl aminopeptidase) from Escherichia coli and conformational change of methionine 260 involved in substrate recognition., Ito K, Nakajima Y, Onohara Y, Takeo M, Nakashima K, Matsubara F, Ito T, Yoshimoto T, J Biol Chem. 2006 Nov 3;281(44):33664-76. Epub 2006 Aug 2. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16885166 16885166]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Membrane alanyl aminopeptidase]]
[[Category: Membrane alanyl aminopeptidase]]
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[[Category: zinc]]
[[Category: zinc]]


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Revision as of 17:30, 20 March 2008

File:2dq6.gif


PDB ID 2dq6

Drag the structure with the mouse to rotate
, resolution 1.50Å
Ligands: and
Gene: pepN (Escherichia coli)
Activity: Membrane alanyl aminopeptidase, with EC number 3.4.11.2
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of Aminopeptidase N from Escherichia coli


OverviewOverview

Aminopeptidase N from Escherichia coli is a broad specificity zinc exopeptidase belonging to aminopeptidase clan MA, family M1. The structures of the ligand-free form and the enzyme-bestatin complex were determined at 1.5- and 1.6-A resolution, respectively. The enzyme is composed of four domains: an N-terminal beta-domain (Met(1)-Asp(193)), a catalytic domain (Phe(194)-Gly(444)), a middle beta-domain (Thr(445)-Trp(546)), and a C-terminal alpha-domain (Ser(547)-Ala(870)). The structure of the catalytic domain exhibits similarity to thermolysin, and a metal-binding motif (HEXXHX(18)E) is found in the domain. The zinc ion is coordinated by His(297), His(301), Glu(320), and a water molecule. The groove on the catalytic domain that contains the active site is covered by the C-terminal alpha-domain, and a large cavity is formed inside the protein. However, there exists a small hole at the center of the C-terminal alpha-domain. The N terminus of bestatin is recognized by Glu(121) and Glu(264), which are located in the N-terminal and catalytic domains, respectively. Glu(298) and Tyr(381), located near the zinc ion, are considered to be involved in peptide cleavage. A difference revealed between the ligand-free form and the enzyme-bestatin complex indicated that Met(260) functions as a cushion to accept substrates with different N-terminal residue sizes, resulting in the broad substrate specificity of this enzyme.

About this StructureAbout this Structure

2DQ6 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of aminopeptidase N (proteobacteria alanyl aminopeptidase) from Escherichia coli and conformational change of methionine 260 involved in substrate recognition., Ito K, Nakajima Y, Onohara Y, Takeo M, Nakashima K, Matsubara F, Ito T, Yoshimoto T, J Biol Chem. 2006 Nov 3;281(44):33664-76. Epub 2006 Aug 2. PMID:16885166

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