3fm3: Difference between revisions
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==Crystal structure of an Encephalitozoon cuniculi methionine aminopeptidase type 2== | ==Crystal structure of an Encephalitozoon cuniculi methionine aminopeptidase type 2== | ||
<StructureSection load='3fm3' size='340' side='right' caption='[[3fm3]], [[Resolution|resolution]] 2.18Å' scene=''> | <StructureSection load='3fm3' size='340' side='right'caption='[[3fm3]], [[Resolution|resolution]] 2.18Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3fm3]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3fm3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Encephalitozoon_cuniculi Encephalitozoon cuniculi]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2nw5 2nw5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FM3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FM3 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.18Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |||
<tr id=' | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3fm3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fm3 OCA], [https://pdbe.org/3fm3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fm3 RCSB], [https://www.ebi.ac.uk/pdbsum/3fm3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fm3 ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/MAP2_ENCCU MAP2_ENCCU] Cotranslationally 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).[HAMAP-Rule:MF_03175]<ref>PMID:14736176</ref> <ref>PMID:16004378</ref> <ref>PMID:16917013</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fm/3fm3_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fm/3fm3_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | </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=3fm3 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
| Line 29: | Line 28: | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3fm3" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Aminopeptidase|Aminopeptidase]] | *[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 37: | Line 37: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Encephalitozoon cuniculi]] | [[Category: Encephalitozoon cuniculi]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Adams | [[Category: Adams J]] | ||
[[Category: Almo | [[Category: Almo SC]] | ||
[[Category: Alvarado | [[Category: Alvarado JJ]] | ||
[[Category: Burley | [[Category: Burley SK]] | ||
[[Category: Russell M]] | |||
[[Category: Russell | [[Category: Toro R]] | ||
[[Category: Toro | [[Category: Weiss LM]] | ||
[[Category: Weiss | [[Category: Zhang A]] | ||
[[Category: Zhang | |||
Latest revision as of 09:48, 6 September 2023
Crystal structure of an Encephalitozoon cuniculi methionine aminopeptidase type 2Crystal structure of an Encephalitozoon cuniculi methionine aminopeptidase type 2
Structural highlights
FunctionMAP2_ENCCU Cotranslationally 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).[HAMAP-Rule:MF_03175][1] [2] [3] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedMicrosporidia are protists that have been reported to cause infections in both vertebrates and invertebrates. They have emerged as human pathogens particularly in patients that are immunosuppressed and cases of gastrointestinal infection, encephalitis, keratitis, sinusitis, myositis and disseminated infection are well described in the literature. While benzimidazoles are active against many species of microsporidia, these drugs do not have significant activity against Enterocytozoon bieneusi. Fumagillin and its analogues have been demonstrated to have activity invitro and in animal models of microsporidiosis and human infections due to E. bieneusi. Fumagillin and its analogues inhibit methionine aminopeptidase type 2. Encephalitozoon cuniculi MetAP2 (EcMetAP2) was cloned and expressed as an active enzyme using a baculovirus system. The crystal structure of EcMetAP2 was determined with and without the bound inhibitors fumagillin and TNP-470. This structure classifies EcMetAP2 as a member of the MetAP2c family. The EcMetAP2 structure was used to generate a homology model of the E. bieneusi MetAP2. Comparison of microsporidian MetAP2 structures with human MetAP2 provides insights into the design of inhibitors that might exhibit specificity for microsporidian MetAP2. Structure of a microsporidian methionine aminopeptidase type 2 complexed with fumagillin and TNP-470.,Alvarado JJ, Nemkal A, Sauder JM, Russell M, Akiyoshi DE, Shi W, Almo SC, Weiss LM Mol Biochem Parasitol. 2009 Dec;168(2):158-67. Epub 2009 Aug 4. PMID:19660503[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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