2p99: Difference between revisions

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[[Image:2p99.png|left|200px]]


{{STRUCTURE_2p99|  PDB=2p99  |  SCENE=  }}
==E. coli methionine aminopeptidase monometalated with inhibitor YE6==
 
<StructureSection load='2p99' size='340' side='right'caption='[[2p99]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
===E. coli methionine aminopeptidase monometalated with inhibitor YE6===
== Structural highlights ==
 
<table><tr><td colspan='2'>[[2p99]] 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=2P99 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2P99 FirstGlance]. <br>
{{ABSTRACT_PUBMED_17948983}}
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=YE6:5-(2-CHLOROPHENYL)FURAN-2-CARBOHYDRAZIDE'>YE6</scene></td></tr>
==About this Structure==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2p99 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p99 OCA], [https://pdbe.org/2p99 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2p99 RCSB], [https://www.ebi.ac.uk/pdbsum/2p99 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2p99 ProSAT]</span></td></tr>
[[2p99]] is a 1 chain structure with 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=2P99 OCA].  
</table>
== 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/p9/2p99_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=2p99 ConSurf].
<div style="clear:both"></div>


==See Also==
==See Also==
*[[Aminopeptidase|Aminopeptidase]]
*[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:017948983</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Methionyl aminopeptidase]]
[[Category: Large Structures]]
[[Category: Ye, Q.]]
[[Category: Ye Q]]
[[Category: Enzyme-inhibitor complex]]
[[Category: Hydrolase]]
[[Category: Metalloenzyme]]
[[Category: Monometalated]]
[[Category: Mononuclear]]

Latest revision as of 12:08, 21 February 2024

E. coli methionine aminopeptidase monometalated with inhibitor YE6E. coli methionine aminopeptidase monometalated with inhibitor YE6

Structural highlights

2p99 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 1.8Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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][1] [2]

Evolutionary Conservation

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

See Also

References

  1. ↑ Xiao Q, Zhang F, Nacev BA, Liu JO, Pei D. Protein N-terminal processing: substrate specificity of Escherichia coli and human methionine aminopeptidases. Biochemistry. 2010 Jul 6;49(26):5588-99. doi: 10.1021/bi1005464. PMID:20521764 doi:http://dx.doi.org/10.1021/bi1005464
  2. ↑ Ben-Bassat A, Bauer K, Chang SY, Myambo K, Boosman A, Chang S. Processing of the initiation methionine from proteins: properties of the Escherichia coli methionine aminopeptidase and its gene structure. J Bacteriol. 1987 Feb;169(2):751-7. PMID:3027045

2p99, resolution 1.80Å

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