3fm3: Difference between revisions

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[[Image:3fm3.png|left|200px]]


{{STRUCTURE_3fm3| PDB=3fm3 | SCENE= }}
==Crystal structure of an Encephalitozoon cuniculi methionine aminopeptidase type 2==
<StructureSection load='3fm3' size='340' side='right'caption='[[3fm3]], [[Resolution|resolution]] 2.18&Aring;' scene=''>
== Structural highlights ==
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.18&#8491;</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='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>
</table>
== 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 ==
[[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/fm/3fm3_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=3fm3 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Microsporidia 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.


===Crystal structure of an Encephalitozoon cuniculi methionine aminopeptidase type 2===
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<ref>PMID:19660503</ref>


{{ABSTRACT_PUBMED_19660503}}
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
==About this Structure==
<div class="pdbe-citations 3fm3" style="background-color:#fffaf0;"></div>
[[3fm3]] is a 2 chain structure of [[Aminopeptidase]] with sequence from [http://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].


==See Also==
==See Also==
*[[Aminopeptidase|Aminopeptidase]]
*[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:019660503</ref><references group="xtra"/>
__TOC__
[[Category: Encephalitozoon cuniculi]]
</StructureSection>
[[Category: Methionyl aminopeptidase]]
[[Category: Adams, J.]]
[[Category: Almo, S C.]]
[[Category: Alvarado, J J.]]
[[Category: Burley, S K.]]
[[Category: NYSGXRC, New York SGX Research Center for Structural Genomics.]]
[[Category: Russell, M.]]
[[Category: Toro, R.]]
[[Category: Weiss, L M.]]
[[Category: Zhang, A.]]
[[Category: Aminopeptidase]]
[[Category: Cobalt]]
[[Category: Encephalitozoon cuniculi]]
[[Category: Encephalitozoon cuniculi]]
[[Category: Hydrolase]]
[[Category: Large Structures]]
[[Category: Metal-binding]]
[[Category: Adams J]]
[[Category: Metap2]]
[[Category: Almo SC]]
[[Category: Methionine aminopeptidase type2]]
[[Category: Alvarado JJ]]
[[Category: New york sgx research center for structural genomic]]
[[Category: Burley SK]]
[[Category: Nysgxrc]]
[[Category: Russell M]]
[[Category: Protease]]
[[Category: Toro R]]
[[Category: Protein structure initiative]]
[[Category: Weiss LM]]
[[Category: Psi-2]]
[[Category: Zhang A]]
[[Category: Structural genomic]]

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

3fm3 is a 2 chain structure with sequence from Encephalitozoon cuniculi. This structure supersedes the now removed PDB entry 2nw5. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.18Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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][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 PubMed

Microsporidia 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 Also

References

  1. Weiss LM, Zhou GC, Zhang H. Characterization of recombinant microsporidian methionine aminopeptidase type 2. J Eukaryot Microbiol. 2003;50 Suppl:597-9. PMID:14736176 doi:10.1111/j.1550-7408.2003.tb00643.x
  2. Zhang H, Huang H, Cali A, Takvorian PM, Feng X, Zhou G, Weiss LM. Investigations into microsporidian methionine aminopeptidase type 2: a therapeutic target for microsporidiosis. Folia Parasitol (Praha). 2005 May;52(1-2):182-92. PMID:16004378 doi:10.14411/fp.2005.023
  3. Upadhya R, Zhang HS, Weiss LM. System for expression of microsporidian methionine amino peptidase type 2 (MetAP2) in the yeast Saccharomyces cerevisiae. Antimicrob Agents Chemother. 2006 Oct;50(10):3389-95. PMID:16917013 doi:10.1128/AAC.00726-06
  4. Alvarado JJ, Nemkal A, Sauder JM, Russell M, Akiyoshi DE, Shi W, Almo SC, Weiss LM. Structure of a microsporidian methionine aminopeptidase type 2 complexed with fumagillin and TNP-470. Mol Biochem Parasitol. 2009 Dec;168(2):158-67. Epub 2009 Aug 4. PMID:19660503 doi:10.1016/j.molbiopara.2009.07.008

3fm3, resolution 2.18Å

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