2gg3: Difference between revisions

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[[Image:2gg3.png|left|200px]]


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==Novel bacterial methionine aminopeptidase inhibitors==
The line below this paragraph, containing "STRUCTURE_2gg3", creates the "Structure Box" on the page.
<StructureSection load='2gg3' size='340' side='right'caption='[[2gg3]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2gg3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GG3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GG3 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.45&#8491;</td></tr>
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<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=U13:4-(4-FLUORO-PHENYLAZO)-5-IMINO-5H-PYRAZOL-3-YLAMINE'>U13</scene></td></tr>
{{STRUCTURE_2gg3|  PDB=2gg3  |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2gg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gg3 OCA], [https://pdbe.org/2gg3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gg3 RCSB], [https://www.ebi.ac.uk/pdbsum/2gg3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gg3 ProSAT]</span></td></tr>
</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>
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    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gg/2gg3_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=2gg3 ConSurf].
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== Publication Abstract from PubMed ==
In this article we describe the application of structural biology methods to the discovery of novel potent inhibitors of methionine aminopeptidases. These enzymes are employed by the cells to cleave the N-terminal methionine from nascent peptides and proteins. As this is one of the critical steps in protein maturation, it is very likely that inhibitors of these enzymes may prove useful as novel antibacterial agents. Involvement of crystallography at the very early stages of the inhibitor design process resulted in serendipitous discovery of a new inhibitor class, the pyrazole-diamines. Atomic-resolution structures of several inhibitors bound to the enzyme illuminate a new mode of inhibitor binding.


===Novel bacterial methionine aminopeptidase inhibitors===
Serendipitous discovery of novel bacterial methionine aminopeptidase inhibitors.,Evdokimov AG, Pokross M, Walter RL, Mekel M, Barnett BL, Amburgey J, Seibel WL, Soper SJ, Djung JF, Fairweather N, Diven C, Rastogi V, Grinius L, Klanke C, Siehnel R, Twinem T, Andrews R, Curnow A Proteins. 2007 Feb 15;66(3):538-46. PMID:17120228<ref>PMID:17120228</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2gg3" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_17120228}}, adds the Publication Abstract to the page
*[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 17120228 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_17120228}}
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</StructureSection>
==About this Structure==
[[Category: Escherichia coli K-12]]
2GG3 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=2GG3 OCA].
[[Category: Large Structures]]
 
[[Category: Evdokimov AG]]
==Reference==
[[Category: Mekel M]]
Serendipitous discovery of novel bacterial methionine aminopeptidase inhibitors., Evdokimov AG, Pokross M, Walter RL, Mekel M, Barnett BL, Amburgey J, Seibel WL, Soper SJ, Djung JF, Fairweather N, Diven C, Rastogi V, Grinius L, Klanke C, Siehnel R, Twinem T, Andrews R, Curnow A, Proteins. 2007 Feb 15;66(3):538-46. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17120228 17120228]
[[Category: Pokross ME]]
[[Category: Escherichia coli]]
[[Category: Walter RL]]
[[Category: Methionyl aminopeptidase]]
[[Category: Single protein]]
[[Category: Evdokimov, A G.]]
[[Category: Mekel, M.]]
[[Category: Pokross, M E.]]
[[Category: Walter, R L.]]
[[Category: Antibacterial]]
[[Category: Map inhibitor]]
[[Category: Methionine amino peptidase]]
[[Category: Pita-bread fold]]
 
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