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[[Image:2dq6.gif|left|200px]]<br /><applet load="2dq6" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2dq6, resolution 1.50&Aring;" />
'''Crystal Structure of Aminopeptidase N from Escherichia coli'''<br />


==Overview==
==Crystal Structure of Aminopeptidase N from Escherichia coli==
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.
<StructureSection load='2dq6' size='340' side='right'caption='[[2dq6]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2dq6]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DQ6 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2dq6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dq6 OCA], [https://pdbe.org/2dq6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dq6 RCSB], [https://www.ebi.ac.uk/pdbsum/2dq6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dq6 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/AMPN_ECOLI AMPN_ECOLI] Aminopeptidase N is involved in the degradation of intracellular peptides generated by protein breakdown during normal growth as well as in response to nutrient starvation.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dq/2dq6_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2dq6 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
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].
*[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
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]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Membrane alanyl aminopeptidase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Ito K]]
[[Category: Ito, K.]]
[[Category: Nakajima Y]]
[[Category: Nakajima, Y.]]
[[Category: Onohara Y]]
[[Category: Onohara, Y.]]
[[Category: Yoshimoto T]]
[[Category: Yoshimoto, T.]]
[[Category: SO4]]
[[Category: ZN]]
[[Category: clan ma]]
[[Category: family m1]]
[[Category: gluzincin metallopeptidase]]
[[Category: zinc]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:01:24 2008''

Latest revision as of 16:47, 13 March 2024

Crystal Structure of Aminopeptidase N from Escherichia coliCrystal Structure of Aminopeptidase N from Escherichia coli

Structural highlights

2dq6 is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.5Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

AMPN_ECOLI Aminopeptidase N is involved in the degradation of intracellular peptides generated by protein breakdown during normal growth as well as in response to nutrient starvation.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

2dq6, resolution 1.50Å

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