We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

3mn8

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (02:08, 21 November 2024) (edit) (undo)
 
(9 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:3mn8.jpg|left|200px]]
 
-
<!--
+
==Structure of Drosophila melanogaster carboxypeptidase D isoform 1B short==
-
The line below this paragraph, containing "STRUCTURE_3mn8", creates the "Structure Box" on the page.
+
<StructureSection load='3mn8' size='340' side='right'caption='[[3mn8]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[3mn8]] is a 4 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=3MN8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MN8 FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
-
-->
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GEM:(2-GUANIDINOETHYLMERCAPTO)SUCCINIC+ACID'>GEM</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-
{{STRUCTURE_3mn8| PDB=3mn8 | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3mn8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mn8 OCA], [https://pdbe.org/3mn8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mn8 RCSB], [https://www.ebi.ac.uk/pdbsum/3mn8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mn8 ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/CBPD_DROME CBPD_DROME] Metallocarboxypeptidase that catalyzes the release of C-terminal arginine or lysine residues from peptides and proteins (PubMed:12393882, PubMed:16556608, PubMed:20386952, PubMed:20600119, PubMed:31309630). Functionally important for processing a broad range of proteins including growth factors, peptide hormones (such as Akh) and neuropeptides (PubMed:16556608, PubMed:20386952, PubMed:20600119, PubMed:27430952, PubMed:31309630). Consequently, it is involved in a wide range of processes including viability, memory formation, locomotive activity, wing formation, and peptide-regulated behaviors such as starvation-induced hyperactivity, appetitive gustatory preference, and cold and ethanol sensitivity (PubMed:20386952, PubMed:20600119, PubMed:27430952, PubMed:31309630). Key enzyme in neuropeptide processing (PubMed:31309630). Involved in regulation of memory formation, possibly via the insulin pathway in neurosecretory cells (PubMed:27430952).<ref>PMID:12393882</ref> <ref>PMID:16556608</ref> <ref>PMID:20386952</ref> <ref>PMID:20600119</ref> <ref>PMID:27430952</ref> <ref>PMID:31309630</ref>
 +
== 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/mn/3mn8_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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/main_output.php?pdb_ID=3mn8 ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Drosophila melanogaster silver gene is the ortholog of the coding gene of mammalian carboxypeptidase D (CPD). The silver gene gives rise to eight different splicing variants of differing length that can contain up to three homologous repeats. Among the protein variants encoded, the short form 1B alias DmCPD1Bs (D. melanogaster CPD variant 1B short) is necessary and sufficient for viability of the fruit fly. It has one single repeat, it is active against standard peptide substrates, and it is localized to the secretory pathway. In this work, the enzyme was found as a monomer in solution and as a homodimer in the crystal structure, which features a protomer with an N-terminal 311-residue catalytic domain of alpha/beta-hydrolase fold and a C-terminal 84-residue all-beta transthyretin-like domain. Overall, DmCPD1Bs conforms to the structure of N/E-type funnelins/M14B metallopeptidases, but it has two unique structural elements potentially involved in regulation of its activity: (i) two contiguous surface cysteines that may become palmitoylated and target the enzyme to membranes, thus providing control through localization, and (ii) a surface hot spot targetable by peptidases that would provide a regulatory mechanism through proteolytic inactivation. Given that the fruit fly possesses orthologs of only two out of the five proteolytically competent N/E-type funnelins found in higher vertebrates, DmCPD1Bs may represent a functional analog of at least one of the missing mammalian CPs.
-
===Structure of Drosophila melanogaster carboxypeptidase D isoform 1B short===
+
Structure-function analysis of the short splicing variant carboxypeptidase encoded by Drosophila melanogaster silver.,Tanco S, Arolas JL, Guevara T, Lorenzo J, Aviles FX, Gomis-Ruth FX J Mol Biol. 2010 Aug 20;401(3):465-77. Epub 2010 Jun 25. PMID:20600119<ref>PMID:20600119</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 3mn8" style="background-color:#fffaf0;"></div>
-
<!--
+
==See Also==
-
The line below this paragraph, {{ABSTRACT_PUBMED_20600119}}, adds the Publication Abstract to the page
+
*[[Carboxypeptidase 3D structures|Carboxypeptidase 3D structures]]
-
(as it appears on PubMed at http://www.pubmed.gov), where 20600119 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_20600119}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
-
3MN8 is a 4 chains structure with sequences from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MN8 OCA].
+
-
 
+
-
==Reference==
+
-
<ref group="xtra">PMID:20600119</ref><references group="xtra"/>
+
[[Category: Drosophila melanogaster]]
[[Category: Drosophila melanogaster]]
-
[[Category: Arolas, J L.]]
+
[[Category: Large Structures]]
-
[[Category: Aviles, F X.]]
+
[[Category: Arolas JL]]
-
[[Category: Gomis-Ruth, F X.]]
+
[[Category: Aviles FX]]
-
[[Category: Guevara, T.]]
+
[[Category: Gomis-Ruth FX]]
-
[[Category: Lorenzo, J.]]
+
[[Category: Guevara T]]
-
[[Category: Tanco, S.]]
+
[[Category: Lorenzo J]]
-
[[Category: All-beta transthyretin-like domain]]
+
[[Category: Tanco S]]
-
[[Category: C-terminal]]
+
-
[[Category: Catalytic domain of alpha/beta-hydrolase fold]]
+
-
[[Category: Hydrolase]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 28 12:39:26 2010''
+

Current revision

Structure of Drosophila melanogaster carboxypeptidase D isoform 1B short

PDB ID 3mn8

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3mn8"
Personal tools