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| | <StructureSection load='5zie' size='340' side='right'caption='[[5zie]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='5zie' size='340' side='right'caption='[[5zie]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5zie]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Legph Legph]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZIE OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5ZIE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5zie]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Legionella_pneumophila_subsp._pneumophila_str._Philadelphia_1 Legionella pneumophila subsp. pneumophila str. Philadelphia 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZIE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZIE FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ASP:ASPARTIC+ACID'>ASP</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]] 2Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Membrane_alanyl_aminopeptidase Membrane alanyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.2 3.4.11.2] </span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ASP:ASPARTIC+ACID'>ASP</scene></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=5zie FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zie OCA], [http://pdbe.org/5zie PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zie RCSB], [http://www.ebi.ac.uk/pdbsum/5zie PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zie ProSAT]</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=5zie FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zie OCA], [https://pdbe.org/5zie PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zie RCSB], [https://www.ebi.ac.uk/pdbsum/5zie PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zie ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q5ZVE3_LEGPH Q5ZVE3_LEGPH] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Legph]] | + | [[Category: Legionella pneumophila subsp. pneumophila str. Philadelphia 1]] |
| - | [[Category: Membrane alanyl aminopeptidase]]
| + | [[Category: Addlagatta A]] |
| - | [[Category: Addlagatta, A]] | + | [[Category: Marapaka AK]] |
| - | [[Category: Marapaka, A K]] | + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: M1 class aminopeptidase]]
| + | |
| Structural highlights
Function
Q5ZVE3_LEGPH
Publication Abstract from PubMed
Aminopeptidases catalyze the hydrolysis of amino acids from the N-terminus of protein or peptide substrates. M1 family aminopeptidases are important for the pathogenicity of bacteria and play critical role in many physiological processes such as protein maturation, regulation of peptide hormone levels in humans. Most of the M1 family aminopeptidases reported till date display broad substrates specificity, mostly specific to basic and hydrophobic residues. In the current study we report the discovery of a novel M1 class aminopeptidase from Legionella pneumophila (LePepA), which cleaves only acidic residues. Biochemical and structural studies reveal that the S1 pocket is polar and positively charged. Bioinformatic analysis suggests that such active site is unique to only Legionella species and probably evolved for special needs of the microbe. Given its specific activity, LePepA could be useful in specific biotechnological applications.
Discovery, Structural and Biochemical Studies of a rare Glu/Asp Specific M1 Class Aminopeptidase from Legionella pneumophila.,Marapaka AK, Pillalamarri V, Gumpena R, Haque N, Bala SC, Jangam A, Addlagatta A Int J Biol Macromol. 2018 Aug 30;120(Pt A):1111-1118. doi:, 10.1016/j.ijbiomac.2018.08.172. PMID:30172821[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Marapaka AK, Pillalamarri V, Gumpena R, Haque N, Bala SC, Jangam A, Addlagatta A. Discovery, Structural and Biochemical Studies of a rare Glu/Asp Specific M1 Class Aminopeptidase from Legionella pneumophila. Int J Biol Macromol. 2018 Aug 30;120(Pt A):1111-1118. doi:, 10.1016/j.ijbiomac.2018.08.172. PMID:30172821 doi:http://dx.doi.org/10.1016/j.ijbiomac.2018.08.172
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