3fvz: Difference between revisions
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[[Image: | ==Structure of Peptidyl-alpha-hydroxyglycine alpha-Amidating Lyase (PAL)== | ||
<StructureSection load='3fvz' size='340' side='right' caption='[[3fvz]], [[Resolution|resolution]] 2.35Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3fvz]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FVZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3FVZ FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3fw0|3fw0]], [[1phm|1phm]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Pam ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylamidoglycolate_lyase Peptidylamidoglycolate lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.2.5 4.3.2.5] </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=3fvz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fvz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3fvz RCSB], [http://www.ebi.ac.uk/pdbsum/3fvz PDBsum]</span></td></tr> | |||
</table> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fv/3fvz_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Many neuropeptides and peptide hormones require amidation of their carboxy terminal for full biological activity. The enzyme peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL; EC 4.3.2.5) catalyzes the second and last step of this reaction, N-dealkylation of the peptidyl-alpha-hydroxyglycine to generate the alpha-amidated peptide and glyoxylate. Here we report the X-ray crystal structure of the PAL catalytic core (PALcc) alone and in complex with the nonpeptidic substrate alpha-hydroxyhippuric acid. The structures show that PAL folds as a six-bladed beta-propeller. The active site is formed by a Zn(II) ion coordinated by three histidine residues; the substrate binds to this site with its alpha-hydroxyl group coordinated to the Zn(II) ion. The structures also reveal a tyrosine residue (Tyr(654)) at the active site as the catalytic base for hydroxyl deprotonation, an unusual role for tyrosine. A reaction mechanism is proposed based on this structural data and validated by biochemical analysis of site-directed PALcc mutants. | |||
Amidation of bioactive peptides: the structure of the lyase domain of the amidating enzyme.,Chufan EE, De M, Eipper BA, Mains RE, Amzel LM Structure. 2009 Jul 15;17(7):965-73. PMID:19604476<ref>PMID:19604476</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Peptidylamidoglycolate lyase]] | [[Category: Peptidylamidoglycolate lyase]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Amzel, L M | [[Category: Amzel, L M]] | ||
[[Category: Chufan, E E | [[Category: Chufan, E E]] | ||
[[Category: De, M | [[Category: De, M]] | ||
[[Category: Eipper, B A | [[Category: Eipper, B A]] | ||
[[Category: Mains, R E | [[Category: Mains, R E]] | ||
[[Category: Beta propeller]] | [[Category: Beta propeller]] | ||
[[Category: Cleavage on pair of basic residue]] | [[Category: Cleavage on pair of basic residue]] | ||
Revision as of 10:14, 3 December 2014
Structure of Peptidyl-alpha-hydroxyglycine alpha-Amidating Lyase (PAL)
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Proteopedia Page Contributors and Editors (what is this?)
Categories:
- Peptidylamidoglycolate lyase
- Rattus norvegicus
- Amzel, L M
- Chufan, E E
- De, M
- Eipper, B A
- Mains, R E
- Beta propeller
- Cleavage on pair of basic residue
- Cytoplasmic vesicle
- Glycoprotein
- Hg-mad
- Lyase
- Membrane
- Metal-binding
- Monooxygenase
- Multifunctional enzyme
- Oxidoreductase
- Peptide amidation
- Phosphoprotein
- Sulfation
- Transmembrane
- Vitamin c
- Zn-mad
