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4km3

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Revision as of 11:44, 5 August 2016

Discovery of a novel structural motif in methionine aminopeptidase from Streptococci with possible post-translational modification

Structural highlights

4km3 is a 2 chain structure with sequence from Strps. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	map, SPCG_1194 (STRPS)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[B2IQ22_STRPS] 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 (By similarity).[HAMAP-Rule:MF_01974]

Publication Abstract from PubMed

Protein N-terminal methionine excision is an essential co-translational process that occurs in the cytoplasm of all organisms. About 60-70% of the newly synthesized proteins undergo this modification. Enzyme responsible for the removal of initiator methionine is methionine aminopeptidase (MetAP), which is a dinuclear metalloprotease. This protein is conserved through all forms of life from bacteria to human except viruses. MetAP is classified into two isoforms, Type I and II. Removal of the map gene or chemical inhibition is lethal to bacteria and to human cell lines, suggesting that MetAP could be a good drug target. In the present study we describe the discovery of a new genetic variant of the Type I MetAP that is present predominantly in the streptococci bacteria. There are two inserts (insert one: 27 amino acids and insert two: four residues) within the catalytic domain. Possible glycosylation and phosphorylation posttranslational modification sites are identified in the 'insert one'. Biochemical characterization suggests that this enzyme behaves similar to other MetAPs in terms of substrate specificity. Crystal structure Type Ia MetAP from Streptococcus pneumoniae (SpMetAP1a) revealed that it contains two molecules in the asymmetric unit and well ordered inserts with structural features that corroborate the possible posttranslational modification. Both the new inserts found in the SpMetAP1a structurally align with the P-X-X-P motif found in the M. tuberculosis and human Type I MetAPs as well as the 60 amino acid insert in the human Type II enzyme suggesting possible common function. In addition, one of the beta-hairpins within in the catalytic domain undergoes a flip placing a residue which is essential for enzyme activity away from the active site and the beta-hairpin loop of this secondary structure in the active site obstructing substrate binding. This is the first example of a MetAP crystallizing in the inactive form.

Discovery of a new genetic variant of methionine aminopeptidase from Streptococci with possible post-translational modifications: biochemical and structural characterization.,Arya T, Kishor C, Saddanapu V, Reddi R, Addlagatta A PLoS One. 2013 Oct 4;8(10):e75207. doi: 10.1371/journal.pone.0075207. PMID:24124477^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Arya T, Kishor C, Saddanapu V, Reddi R, Addlagatta A. Discovery of a new genetic variant of methionine aminopeptidase from Streptococci with possible post-translational modifications: biochemical and structural characterization. PLoS One. 2013 Oct 4;8(10):e75207. doi: 10.1371/journal.pone.0075207. PMID:24124477 doi:http://dx.doi.org/10.1371/journal.pone.0075207

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4km3"

Categories: Strps | Addlagatta, A | Arya, T | Classification | Hydrolase

@@ Line 1: / Line 1: @@
 ==Discovery of a novel structural motif in methionine aminopeptidase from Streptococci with possible post-translational modification==
 <StructureSection load='4km3' size='340' side='right' caption='[[4km3]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[4km3]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Strps Strps]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KM3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4KM3 FirstGlance]. <br>
 </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">map, SPCG_1194 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=516950 STRPS])</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=4km3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4km3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4km3 RCSB], [http://www.ebi.ac.uk/pdbsum/4km3 PDBsum]</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=4km3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4km3 OCA], [http://pdbe.org/4km3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4km3 RCSB], [http://www.ebi.ac.uk/pdbsum/4km3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4km3 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 16: / Line 17: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4km3" style="background-color:#fffaf0;"></div>
 ==See Also==

4km3

From Proteopedia

Revision as of 11:44, 5 August 2016

Discovery of a novel structural motif in methionine aminopeptidase from Streptococci with possible post-translational modification

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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