2kyt

From Proteopedia

(Difference between revisions)

Revision as of 14:22, 22 December 2016

Solution structure of the H-REV107 N-terminal domain

Structural highlights

2kyt is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Activity:	Phospholipase A(2), with EC number 3.1.1.4
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[HRSL3_HUMAN] Exhibits PLA1/2 activity, catalyzing the calcium-independent hydrolysis of acyl groups in various phosphatidylcholines (PC) and phosphatidylethanolamine (PE). For most substrates, PLA1 activity is much higher than PLA2 activity. Specifically catalyzes the release of fatty acids from phospholipids in adipose tissue (By similarity). N- and O-acylation activity is hardly detectable. Might decrease protein phosphatase 2A (PP2A) activity.^[1] ^[2]

Publication Abstract from PubMed

H-REV107 is a Ca(2+)-independent phospholipase A(1/2), and it is also a pro-apoptosis protein belonging to the novel class II tumor suppressor family, H-REV107-like family. Here we report the solution structure of the N-terminal catalytic domain of human H-REV107, which has a similar architecture to classical NlpC/P60 domains, even though their fold topologies are different due to circular permutation in the primary sequence. The phospholipase active site possesses a structurally conserved Cys-His-His catalytic triad as found in NlpC/P60 peptidases, indicating H-REV107 should adopt a similar catalytic mechanism towards phospholipid substrates to that of NlpC/P60 peptidases towards peptides. As H-REV107 is highly similar to lecithin retinol acyltransferase, our study also provides structural insight to this essential enzyme in retinol metabolism.

Solution structure of the N-terminal catalytic domain of human H-REV107--a novel circular permutated NlpC/P60 domain.,Ren X, Lin J, Jin C, Xia B FEBS Lett. 2010 Oct 8;584(19):4222-6. Epub 2010 Sep 17. PMID:20837014^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Nazarenko I, Schafer R, Sers C. Mechanisms of the HRSL3 tumor suppressor function in ovarian carcinoma cells. J Cell Sci. 2007 Apr 15;120(Pt 8):1393-404. Epub 2007 Mar 20. PMID:17374643 doi:http://dx.doi.org/10.1242/jcs.000018
↑ Uyama T, Jin XH, Tsuboi K, Tonai T, Ueda N. Characterization of the human tumor suppressors TIG3 and HRASLS2 as phospholipid-metabolizing enzymes. Biochim Biophys Acta. 2009 Dec;1791(12):1114-24. doi:, 10.1016/j.bbalip.2009.07.001. Epub 2009 Jul 14. PMID:19615464 doi:http://dx.doi.org/10.1016/j.bbalip.2009.07.001
↑ Ren X, Lin J, Jin C, Xia B. Solution structure of the N-terminal catalytic domain of human H-REV107--a novel circular permutated NlpC/P60 domain. FEBS Lett. 2010 Oct 8;584(19):4222-6. Epub 2010 Sep 17. PMID:20837014 doi:10.1016/j.febslet.2010.09.015

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2kyt"

@@ Line 1: / Line 1: @@
-==solution struture of the H-REV107 N-terminal domain==
+==Solution structure of the H-REV107 N-terminal domain==
 <StructureSection load='2kyt' size='340' side='right' caption='[[2kyt]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2kyt]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KYT FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2kyt]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KYT FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PLA2G16, HRASLS3, HREV107 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phospholipase_A(2) Phospholipase A(2)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.4 3.1.1.4] </span></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phospholipase_A(2) Phospholipase A(2)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.4 3.1.1.4] </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=2kyt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kyt OCA], [http://pdbe.org/2kyt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2kyt RCSB], [http://www.ebi.ac.uk/pdbsum/2kyt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2kyt 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=2kyt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kyt OCA], [http://pdbe.org/2kyt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2kyt RCSB], [http://www.ebi.ac.uk/pdbsum/2kyt PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 25: / Line 25: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
 [[Category: Ren, X]]
 [[Category: Xia, B]]

2kyt

From Proteopedia

Revision as of 14:22, 22 December 2016

Solution structure of the H-REV107 N-terminal domain

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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