5ykp: Difference between revisions

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'''Unreleased structure'''


The entry 5ykp is ON HOLD until Paper Publication
==Human methionine aminopeptidase type 1b (F309M mutant) in complex with ovalicin==
 
<StructureSection load='5ykp' size='340' side='right' caption='[[5ykp]], [[Resolution|resolution]] 1.68&Aring;' scene=''>
Authors:  
== Structural highlights ==
 
<table><tr><td colspan='2'>[[5ykp]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YKP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YKP FirstGlance]. <br>
Description:  
</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=OVA:3,4-DIHYDROXY-2-METHOXY-4-METHYL-3-[2-METHYL-3-(3-METHYL-BUT-2-ENYL)+-OXIRANYL]-CYCLOHEXANONE'>OVA</scene></td></tr>
[[Category: Unreleased Structures]]
<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=5ykp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ykp OCA], [http://pdbe.org/5ykp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ykp RCSB], [http://www.ebi.ac.uk/pdbsum/5ykp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ykp ProSAT]</span></td></tr>
</table>
== Function ==
[[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>  
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Methionyl aminopeptidase]]
[[Category: Addlagatta, A]]
[[Category: Arya, T]]
[[Category: Pillalamarri, V]]
[[Category: Enterococcus feacali]]
[[Category: Metal binding protein]]
[[Category: Selective inhibition]]
[[Category: Streptococcal pneumoniae]]

Revision as of 10:50, 17 October 2018

Human methionine aminopeptidase type 1b (F309M mutant) in complex with ovalicinHuman methionine aminopeptidase type 1b (F309M mutant) in complex with ovalicin

Structural highlights

5ykp is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
Activity:Methionyl aminopeptidase, with EC number 3.4.11.18
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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][1] [2]

References

  1. Addlagatta A, Hu X, Liu JO, Matthews BW. Structural basis for the functional differences between type I and type II human methionine aminopeptidases. Biochemistry. 2005 Nov 15;44(45):14741-9. PMID:16274222 doi:10.1021/bi051691k
  2. Hu X, Addlagatta A, Lu J, Matthews BW, Liu JO. Elucidation of the function of type 1 human methionine aminopeptidase during cell cycle progression. Proc Natl Acad Sci U S A. 2006 Nov 28;103(48):18148-53. Epub 2006 Nov 17. PMID:17114291

5ykp, resolution 1.68Å

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