This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2kyt

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (06:50, 1 May 2024) (edit) (undo)
 
(9 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2kyt.png|left|200px]]
 
-
{{STRUCTURE_2kyt| PDB=2kyt | SCENE= }}
+
==Solution structure of the H-REV107 N-terminal domain==
-
 
+
<StructureSection load='2kyt' size='340' side='right'caption='[[2kyt]]' scene=''>
-
===solution struture of the H-REV107 N-terminal domain===
+
== Structural highlights ==
-
 
+
<table><tr><td colspan='2'>[[2kyt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KYT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KYT FirstGlance]. <br>
-
{{ABSTRACT_PUBMED_20837014}}
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2kyt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kyt OCA], [https://pdbe.org/2kyt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kyt RCSB], [https://www.ebi.ac.uk/pdbsum/2kyt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kyt ProSAT]</span></td></tr>
-
==About this Structure==
+
</table>
-
[[2kyt]] is a 1 chain structure of [[Phospholipase A2]] with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KYT OCA].
+
== Function ==
 +
[https://www.uniprot.org/uniprot/PLAT3_HUMAN PLAT3_HUMAN] Exhibits both phospholipase A1/2 and acyltransferase activities (PubMed:19615464, PubMed:19047760, PubMed:22825852, PubMed:22605381, PubMed:26503625). Shows phospholipase A1 (PLA1) and A2 (PLA2) activity, catalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids (PubMed:19615464, PubMed:19047760, PubMed:22825852, PubMed:22605381, PubMed:22923616). For most substrates, PLA1 activity is much higher than PLA2 activity (PubMed:19615464). Shows O-acyltransferase activity,catalyzing the transfer of a fatty acyl group from glycerophospholipid to the hydroxyl group of lysophospholipid (PubMed:19615464). Shows N-acyltransferase activity, catalyzing the calcium-independent transfer of a fatty acyl group at the sn-1 position of phosphatidylcholine (PC) and other glycerophospholipids to the primary amine of phosphatidylethanolamine (PE), forming N-acylphosphatidylethanolamine (NAPE), which serves as precursor for N-acylethanolamines (NAEs) (PubMed:19615464, PubMed:19047760, PubMed:22825852, PubMed:22605381). Exhibits high N-acyltransferase activity and low phospholipase A1/2 activity (PubMed:22825852). Required for complete organelle rupture and degradation that occur during eye lens terminal differentiation, when fiber cells that compose the lens degrade all membrane-bound organelles in order to provide lens with transparency to allow the passage of light. Organelle membrane degradation is probably catalyzed by the phospholipase activity (By similarity).[UniProtKB:Q8R3U1]<ref>PMID:19047760</ref> <ref>PMID:19615464</ref> <ref>PMID:22605381</ref> <ref>PMID:22825852</ref> <ref>PMID:22923616</ref> <ref>PMID:26503625</ref> (Microbial infection) Acts as a host factor for picornaviruses: required during early infection to promote viral genome release into the cytoplasm (PubMed:28077878). May act as a cellular sensor of membrane damage at sites of virus entry, which relocalizes to sites of membrane rupture upon virus unfection (PubMed:28077878). Facilitates safe passage of the RNA away from LGALS8, enabling viral genome translation by host ribosome (PubMed:28077878). May also be involved in initiating pore formation, increasing pore size or in maintaining pores for genome delivery (PubMed:28077878). The lipid-modifying enzyme activity is required for this process (PubMed:28077878).<ref>PMID:28077878</ref>
==See Also==
==See Also==
-
*[[Phospholipase A2|Phospholipase A2]]
+
*[[Phospholipase A2 3D structures|Phospholipase A2 3D structures]]
-
 
+
== References ==
-
==Reference==
+
<references/>
-
<ref group="xtra">PMID:020837014</ref><references group="xtra"/>
+
__TOC__
 +
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Ren, X.]]
+
[[Category: Large Structures]]
-
[[Category: Xia, B.]]
+
[[Category: Ren X]]
-
[[Category: H-rev107]]
+
[[Category: Xia B]]
-
[[Category: Hydrolase]]
+
-
[[Category: N-terminal domain]]
+
-
[[Category: Phospholipase]]
+
-
[[Category: Tumor suppressor]]
+

Current revision

Solution structure of the H-REV107 N-terminal domain

PDB ID 2kyt

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/2kyt"
Personal tools