1yvm

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1yvm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yvm, resolution 1.60&Aring;" /> '''E. coli Methionine A...)
Current revision (07:01, 23 August 2023) (edit) (undo)
 
(16 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1yvm.gif|left|200px]]<br /><applet load="1yvm" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1yvm, resolution 1.60&Aring;" />
 
-
'''E. coli Methionine Aminopeptidase in complex with thiabendazole'''<br />
 
-
==About this Structure==
+
==E. coli Methionine Aminopeptidase in complex with thiabendazole==
-
1YVM 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 CO, NA and TMG as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YVM OCA].
+
<StructureSection load='1yvm' size='340' side='right'caption='[[1yvm]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
 +
== Structural highlights ==
 +
<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>
 +
</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>
 +
<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>
 +
<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>
 +
</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/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>
-
==Reference==
+
==See Also==
-
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=15880695 15880695]
+
*[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]]
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
[[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: CO]]
+
-
[[Category: NA]]
+
-
[[Category: TMG]]
+
-
[[Category: hydrolase(alpha-aminoacylpeptide)]]
+
-
[[Category: inhibitor]]
+
-
[[Category: metal complex]]
+
-
[[Category: methionine aminopeptidase]]
+
-
[[Category: thiabendazole]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:05:04 2007''
+

Current revision

E. coli Methionine Aminopeptidase in complex with thiabendazole

PDB ID 1yvm

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools