|
|
| (One intermediate revision not shown.) |
| Line 3: |
Line 3: |
| | <StructureSection load='1j37' size='340' side='right'caption='[[1j37]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='1j37' size='340' side='right'caption='[[1j37]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1j37]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J37 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1J37 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1j37]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J37 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1J37 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=X8Z:L-CAPTOPRIL'>X8Z</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.4Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1j36|1j36]], [[1j38|1j38]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=X8Z:L-CAPTOPRIL'>X8Z</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidyl-dipeptidase_A Peptidyl-dipeptidase A], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.15.1 3.4.15.1] </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=1j37 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j37 OCA], [https://pdbe.org/1j37 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1j37 RCSB], [https://www.ebi.ac.uk/pdbsum/1j37 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1j37 ProSAT]</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=1j37 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j37 OCA], [http://pdbe.org/1j37 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1j37 RCSB], [http://www.ebi.ac.uk/pdbsum/1j37 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1j37 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ACE_DROME ACE_DROME]] May be involved in the specific maturation or degradation of a number of bioactive peptides. May play a role in the contractions of the heart, gut and testes, and in spermatid differentiation.<ref>PMID:12591244</ref> | + | [https://www.uniprot.org/uniprot/ACE_DROME ACE_DROME] May be involved in the specific maturation or degradation of a number of bioactive peptides. May play a role in the contractions of the heart, gut and testes, and in spermatid differentiation.<ref>PMID:12591244</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 37: |
Line 36: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Drome]] | + | [[Category: Drosophila melanogaster]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Peptidyl-dipeptidase A]]
| + | [[Category: Kim HM]] |
| - | [[Category: Kim, H M]] | + | [[Category: Lee H]] |
| - | [[Category: Lee, H]] | + | [[Category: Lee J-O]] |
| - | [[Category: Lee, J O]] | + | [[Category: Shin DR]] |
| - | [[Category: Shin, D R]] | + | [[Category: Yoo OJ]] |
| - | [[Category: Yoo, O J]] | + | |
| - | [[Category: Angiotensin]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
ACE_DROME May be involved in the specific maturation or degradation of a number of bioactive peptides. May play a role in the contractions of the heart, gut and testes, and in spermatid differentiation.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Angiotensin I-converting enzymes (ACEs) are zinc metallopeptidases that cleave carboxy-terminal dipeptides from short peptide hormones. We have determined the crystal structures of AnCE, a Drosophila homolog of ACE, with and without bound inhibitors to 2.4 A resolution. AnCE contains a large internal channel encompassing the entire protein molecule. This substrate-binding channel is composed of two chambers, reminiscent of a peanut shell. The inhibitor and zinc-binding sites are located in the narrow bottleneck connecting the two chambers. The substrate and inhibitor specificity of AnCE appears to be determined by extensive hydrogen-bonding networks and ionic interactions in the active site channel. The catalytically important zinc ion is coordinated by the conserved Glu395 and histidine residues from a HExxH motif.
Crystal structure of Drosophila angiotensin I-converting enzyme bound to captopril and lisinopril.,Kim HM, Shin DR, Yoo OJ, Lee H, Lee JO FEBS Lett. 2003 Mar 13;538(1-3):65-70. PMID:12633854[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hurst D, Rylett CM, Isaac RE, Shirras AD. The drosophila angiotensin-converting enzyme homologue Ance is required for spermiogenesis. Dev Biol. 2003 Feb 15;254(2):238-47. PMID:12591244
- ↑ Kim HM, Shin DR, Yoo OJ, Lee H, Lee JO. Crystal structure of Drosophila angiotensin I-converting enzyme bound to captopril and lisinopril. FEBS Lett. 2003 Mar 13;538(1-3):65-70. PMID:12633854
|
