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4u73

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==HsMetAP(F309M) IN COMPLEX WITH (amino(phenyl)methyl)phosphonic acid==
==HsMetAP(F309M) IN COMPLEX WITH (amino(phenyl)methyl)phosphonic acid==
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<StructureSection load='4u73' size='340' side='right' caption='[[4u73]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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<StructureSection load='4u73' size='340' side='right'caption='[[4u73]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4u73]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4U73 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4U73 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4u73]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4U73 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4U73 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=Q02:[(R)-AMINO(PHENYL)METHYL]PHOSPHONIC+ACID'>Q02</scene></td></tr>
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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]] 1.8&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4u1b|4u1b]], [[4u69|4u69]], [[4u6c|4u6c]], [[4u6e|4u6e]], [[4u6j|4u6j]], [[4u6w|4u6w]], [[4u6z|4u6z]], [[4u70|4u70]], [[4u71|4u71]], [[4u75|4u75]], [[4u76|4u76]]</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=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=Q02:[(R)-AMINO(PHENYL)METHYL]PHOSPHONIC+ACID'>Q02</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4u73 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u73 OCA], [https://pdbe.org/4u73 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4u73 RCSB], [https://www.ebi.ac.uk/pdbsum/4u73 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4u73 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4u73 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u73 OCA], [http://pdbe.org/4u73 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4u73 RCSB], [http://www.ebi.ac.uk/pdbsum/4u73 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4u73 ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/MAP11_HUMAN MAP11_HUMAN]] 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). Required for normal progression through the cell cycle.[HAMAP-Rule:MF_03174]<ref>PMID:16274222</ref> <ref>PMID:17114291</ref>
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[https://www.uniprot.org/uniprot/MAP11_HUMAN MAP11_HUMAN] 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). Required for normal progression through the cell cycle.[HAMAP-Rule:MF_03174]<ref>PMID:16274222</ref> <ref>PMID:17114291</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The methionine aminopeptidase (MetAP) family is responsible for the cleavage of the initiator methionine from newly synthesized proteins. Currently, there are no small molecule inhibitors that show selectivity toward the bacterial MetAPs compared to the human enzyme. In our current study, we have screened 20 alpha-aminophosphonate derivatives and identified a molecule (compound 15) that selectively inhibits the S. pneumonia MetAP in low micromolar range but not the human enzyme. Further bioinformatics, biochemical, and structural analyses suggested that phenylalanine (F309) in the human enzyme and methionine (M205) in the S. pneumonia MetAP at the analogous position render them with different susceptibilities against the identified inhibitor. X-ray crystal structures of various inhibitors in complex with wild type and F309M enzyme further established the molecular basis for the inhibitor selectivity.
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Identification of the Molecular Basis of Inhibitor Selectivity between the Human and Streptococcal Type I Methionine Aminopeptidases.,Arya T, Reddi R, Kishor C, Ganji RJ, Bhukya S, Gumpena R, McGowan S, Drag M, Addlagatta A J Med Chem. 2015 Mar 12;58(5):2350-7. doi: 10.1021/jm501790e. Epub 2015 Feb 27. PMID:25699713<ref>PMID:25699713</ref>
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==See Also==
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*[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4u73" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Methionyl aminopeptidase]]
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[[Category: Homo sapiens]]
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[[Category: Addlagatta, A]]
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[[Category: Large Structures]]
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[[Category: Arya, T]]
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[[Category: Addlagatta A]]
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[[Category: Hydrolase]]
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[[Category: Arya T]]

Current revision

HsMetAP(F309M) IN COMPLEX WITH (amino(phenyl)methyl)phosphonic acid

PDB ID 4u73

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