5anl: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 3: Line 3:
<StructureSection load='5anl' size='340' side='right' caption='[[5anl]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
<StructureSection load='5anl' size='340' side='right' caption='[[5anl]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5anl]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ANL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ANL FirstGlance]. <br>
<table><tr><td colspan='2'>[[5anl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ANL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ANL FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=RBQ:(8S)-2-(MORPHOLIN-4-YL)-9-[2-(PROPAN-2-YLOXY)ETHYL]-8-(TRIFLUOROMETHYL)-6,7,8,9-TETRAHYDRO-4H-PYRIMIDO[1,2-A]PYRIMIDIN-4-ONE'>RBQ</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=RBQ:(8S)-2-(MORPHOLIN-4-YL)-9-[2-(PROPAN-2-YLOXY)ETHYL]-8-(TRIFLUOROMETHYL)-6,7,8,9-TETRAHYDRO-4H-PYRIMIDO[1,2-A]PYRIMIDIN-4-ONE'>RBQ</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5amw|5amw]], [[5amx|5amx]], [[5amy|5amy]], [[5amz|5amz]], [[5an2|5an2]], [[5an4|5an4]], [[5and|5and]], [[5ane|5ane]], [[5ang|5ang]], [[5ani|5ani]], [[5anj|5anj]], [[5ank|5ank]], [[5ano|5ano]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5amw|5amw]], [[5amx|5amx]], [[5amy|5amy]], [[5amz|5amz]], [[5an2|5an2]], [[5an4|5an4]], [[5and|5and]], [[5ane|5ane]], [[5ang|5ang]], [[5ani|5ani]], [[5anj|5anj]], [[5ank|5ank]], [[5ano|5ano]]</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphatidylinositol_3-kinase Phosphatidylinositol 3-kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.137 2.7.1.137] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphatidylinositol_3-kinase Phosphatidylinositol 3-kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.137 2.7.1.137] </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=5anl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5anl OCA], [http://pdbe.org/5anl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5anl RCSB], [http://www.ebi.ac.uk/pdbsum/5anl PDBsum]</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=5anl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5anl OCA], [http://pdbe.org/5anl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5anl RCSB], [http://www.ebi.ac.uk/pdbsum/5anl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5anl ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
Line 24: Line 24:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Phosphatidylinositol 3-kinase]]
[[Category: Phosphatidylinositol 3-kinase]]
[[Category: Cipriani, F]]
[[Category: Cipriani, F]]

Revision as of 16:08, 16 November 2017

Crystal structure of VPS34 in complex with (2S)-8-((3R)-3- Methylmorpholin-4-yl)-1-(3-methyl-2-oxo- butyl)-2-(trifluoromethyl)-3, 4-dihydro-2H-pyrimido(1,2-a)pyrimidin-6- one, processed with the CrystalDirect automated mounting and cryo-cooling technologyCrystal structure of VPS34 in complex with (2S)-8-((3R)-3- Methylmorpholin-4-yl)-1-(3-methyl-2-oxo- butyl)-2-(trifluoromethyl)-3, 4-dihydro-2H-pyrimido(1,2-a)pyrimidin-6- one, processed with the CrystalDirect automated mounting and cryo-cooling technology

Structural highlights

5anl is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Activity:Phosphatidylinositol 3-kinase, with EC number 2.7.1.137
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PK3C3_HUMAN] Catalytic subunit of the PI3K complex that mediates formation of phosphatidylinositol 3-phosphate which plays a key role in initiation and maturation of autophagosomes. Involved in the transport of lysosomal enzyme precursors to lysosomes. Required for the abcission step in cytokinesis. Required for transport from early to late endosomes.[1] [2] [3]

Publication Abstract from PubMed

Currently, macromolecular crystallography projects often require the use of highly automated facilities for crystallization and X-ray data collection. However, crystal harvesting and processing largely depend on manual operations. Here, a series of new methods are presented based on the use of a low X-ray-background film as a crystallization support and a photoablation laser that enable the automation of major operations required for the preparation of crystals for X-ray diffraction experiments. In this approach, the controlled removal of the mother liquor before crystal mounting simplifies the cryocooling process, in many cases eliminating the use of cryoprotectant agents, while crystal-soaking experiments are performed through diffusion, precluding the need for repeated sample-recovery and transfer operations. Moreover, the high-precision laser enables new mounting strategies that are not accessible through other methods. This approach bridges an important gap in automation and can contribute to expanding the capabilities of modern macromolecular crystallography facilities.

Automated harvesting and processing of protein crystals through laser photoablation.,Zander U, Hoffmann G, Cornaciu I, Marquette JP, Papp G, Landret C, Seroul G, Sinoir J, Rower M, Felisaz F, Rodriguez-Puente S, Mariaule V, Murphy P, Mathieu M, Cipriani F, Marquez JA Acta Crystallogr D Struct Biol. 2016 Apr 1;72(Pt 4):454-66. doi:, 10.1107/S2059798316000954. Epub 2016 Mar 24. PMID:27050125[4]

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

References

  1. Volinia S, Dhand R, Vanhaesebroeck B, MacDougall LK, Stein R, Zvelebil MJ, Domin J, Panaretou C, Waterfield MD. A human phosphatidylinositol 3-kinase complex related to the yeast Vps34p-Vps15p protein sorting system. EMBO J. 1995 Jul 17;14(14):3339-48. PMID:7628435
  2. Stein MP, Feng Y, Cooper KL, Welford AM, Wandinger-Ness A. Human VPS34 and p150 are Rab7 interacting partners. Traffic. 2003 Nov;4(11):754-71. PMID:14617358
  3. Sagona AP, Nezis IP, Pedersen NM, Liestol K, Poulton J, Rusten TE, Skotheim RI, Raiborg C, Stenmark H. PtdIns(3)P controls cytokinesis through KIF13A-mediated recruitment of FYVE-CENT to the midbody. Nat Cell Biol. 2010 Apr;12(4):362-71. doi: 10.1038/ncb2036. Epub 2010 Mar 7. PMID:20208530 doi:http://dx.doi.org/10.1038/ncb2036
  4. Zander U, Hoffmann G, Cornaciu I, Marquette JP, Papp G, Landret C, Seroul G, Sinoir J, Rower M, Felisaz F, Rodriguez-Puente S, Mariaule V, Murphy P, Mathieu M, Cipriani F, Marquez JA. Automated harvesting and processing of protein crystals through laser photoablation. Acta Crystallogr D Struct Biol. 2016 Apr 1;72(Pt 4):454-66. doi:, 10.1107/S2059798316000954. Epub 2016 Mar 24. PMID:27050125 doi:http://dx.doi.org/10.1107/S2059798316000954

5anl, resolution 2.70Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA