1y1n: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
 
Line 3: Line 3:
<StructureSection load='1y1n' size='340' side='right'caption='[[1y1n]], [[Resolution|resolution]] 1.51&Aring;' scene=''>
<StructureSection load='1y1n' size='340' side='right'caption='[[1y1n]], [[Resolution|resolution]] 1.51&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1y1n]] 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=1Y1N OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1Y1N FirstGlance]. <br>
<table><tr><td colspan='2'>[[1y1n]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y1N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y1N FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.51&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">map, mapB ([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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=1y1n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y1n OCA], [https://pdbe.org/1y1n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y1n RCSB], [https://www.ebi.ac.uk/pdbsum/1y1n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y1n ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1y1n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y1n OCA], [http://pdbe.org/1y1n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1y1n RCSB], [http://www.ebi.ac.uk/pdbsum/1y1n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1y1n ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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>
[https://www.uniprot.org/uniprot/MAP12_MYCTU MAP12_MYCTU] 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:19688379</ref> <ref>PMID:20038112</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 38: Line 37:
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Methionyl aminopeptidase]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Addlagatta, A]]
[[Category: Addlagatta A]]
[[Category: Liu, J O]]
[[Category: Liu JO]]
[[Category: Matthews, B W]]
[[Category: Matthews BW]]
[[Category: Omotoso, O]]
[[Category: Omotoso O]]
[[Category: Quillin, M L]]
[[Category: Quillin ML]]
[[Category: Hydrolase]]
[[Category: L24]]
[[Category: Methionine aminopeptidase]]
[[Category: Mtmetap1b]]
[[Category: Pxxp]]
[[Category: Ribosome]]
[[Category: Sh3]]
Retrieved from "https://proteopedia.org/1y1n"