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==Mycobacterium Tuberculosis Methionine aminopeptidase Type 1c in complex with homocysteine-methyl disulfide== | |||
<StructureSection load='4if7' size='340' side='right' caption='[[4if7]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
==Function== | <table><tr><td colspan='2'>[[4if7]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IF7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4IF7 FirstGlance]. <br> | ||
</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=HCM:(2S)-2-AMINO-4-(METHYLDISULFANYL)BUTANOIC+ACID'>HCM</scene></td></tr> | |||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SCH:S-METHYL-THIO-CYSTEINE'>SCH</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4idy|4idy]], [[4iec|4iec]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">map ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884])</td></tr> | |||
<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> | |||
<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=4if7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4if7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4if7 RCSB], [http://www.ebi.ac.uk/pdbsum/4if7 PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/AMPM2_MYCTU AMPM2_MYCTU]] Removes the N-terminal methionine from nascent proteins, when the penultimate amino acid is alanine or proline, but enzyme activity is remarkably low when the second residue is phenylalanine or leucine. With glycine at the second position, Map is more active with a tetrapeptide than with a tripeptide.<ref>PMID:19688379</ref> <ref>PMID:20038112</ref> | [[http://www.uniprot.org/uniprot/AMPM2_MYCTU AMPM2_MYCTU]] Removes the N-terminal methionine from nascent proteins, when the penultimate amino acid is alanine or proline, but enzyme activity is remarkably low when the second residue is phenylalanine or leucine. With glycine at the second position, Map is more active with a tetrapeptide than with a tripeptide.<ref>PMID:19688379</ref> <ref>PMID:20038112</ref> | ||
==See Also== | ==See Also== | ||
*[[Aminopeptidase|Aminopeptidase]] | *[[Aminopeptidase|Aminopeptidase]] | ||
== References == | |||
== | <references/> | ||
<references | __TOC__ | ||
</StructureSection> | |||
[[Category: Methionyl aminopeptidase]] | [[Category: Methionyl aminopeptidase]] | ||
[[Category: Addlagatta, A | [[Category: Addlagatta, A]] | ||
[[Category: Gumpena, R | [[Category: Gumpena, R]] | ||
[[Category: Kishor, C | [[Category: Kishor, C]] | ||
[[Category: Reddi, R | [[Category: Reddi, R]] | ||
[[Category: Aminopeptidase]] | [[Category: Aminopeptidase]] | ||
[[Category: Cobalt]] | [[Category: Cobalt]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Pita-bread fold]] | [[Category: Pita-bread fold]] |
Revision as of 01:44, 26 December 2014
Mycobacterium Tuberculosis Methionine aminopeptidase Type 1c in complex with homocysteine-methyl disulfideMycobacterium Tuberculosis Methionine aminopeptidase Type 1c in complex with homocysteine-methyl disulfide
Structural highlights
Function[AMPM2_MYCTU] Removes the N-terminal methionine from nascent proteins, when the penultimate amino acid is alanine or proline, but enzyme activity is remarkably low when the second residue is phenylalanine or leucine. With glycine at the second position, Map is more active with a tetrapeptide than with a tripeptide.[1] [2] See AlsoReferences
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