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[[Image:1yvm.gif|left|200px]]


{{Structure
==E. coli Methionine Aminopeptidase in complex with thiabendazole==
|PDB= 1yvm |SIZE=350|CAPTION= <scene name='initialview01'>1yvm</scene>, resolution 1.60&Aring;
<StructureSection load='1yvm' size='340' side='right'caption='[[1yvm]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TMG:2-(1,3-THIAZOL-4-YL)-1H-BENZIMIDAZOLE'>TMG</scene>
<table><tr><td colspan='2'>[[1yvm]] 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=1YVM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YVM FirstGlance]. <br>
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Methionyl_aminopeptidase Methionyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.18 3.4.11.18] </span>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
|GENE= map ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TMG:2-(1,3-THIAZOL-4-YL)-1H-BENZIMIDAZOLE'>TMG</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1yvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yvm OCA], [https://pdbe.org/1yvm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yvm RCSB], [https://www.ebi.ac.uk/pdbsum/1yvm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yvm ProSAT]</span></td></tr>
|RELATEDENTRY=[[2mat|2MAT]], [[1xnz|1XNZ]]
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1yvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yvm OCA], [http://www.ebi.ac.uk/pdbsum/1yvm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1yvm RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/MAP1_ECOLI MAP1_ECOLI] Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed.[HAMAP-Rule:MF_01974]<ref>PMID:20521764</ref> <ref>PMID:3027045</ref>
== 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/yv/1yvm_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=1yvm ConSurf].
<div style="clear:both"></div>


'''E. coli Methionine Aminopeptidase in complex with thiabendazole'''
==See Also==
 
*[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]]
 
== References ==
==About this Structure==
<references/>
1YVM 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=1YVM OCA].
__TOC__
 
</StructureSection>
==Reference==
Metal ions as cofactors for the binding of inhibitors to methionine aminopeptidase: a critical view of the relevance of in vitro metalloenzyme assays., Schiffmann R, Heine A, Klebe G, Klein CD, Angew Chem Int Ed Engl. 2005 Jun 6;44(23):3620-3. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15880695 15880695]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Methionyl aminopeptidase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Heine A]]
[[Category: Heine, A.]]
[[Category: Klebe G]]
[[Category: Klebe, G.]]
[[Category: Klein CD]]
[[Category: Klein, C D.]]
[[Category: Schiffmann R]]
[[Category: Schiffmann, R.]]
[[Category: hydrolase(alpha-aminoacylpeptide)]]
[[Category: inhibitor]]
[[Category: metal complex]]
[[Category: methionine aminopeptidase]]
[[Category: thiabendazole]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:24:15 2008''
Retrieved from "https://proteopedia.org/1yvm"