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| | <StructureSection load='6huf' size='340' side='right'caption='[[6huf]], [[Resolution|resolution]] 2.82Å' scene=''> | | <StructureSection load='6huf' size='340' side='right'caption='[[6huf]], [[Resolution|resolution]] 2.82Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6huf]] is a 16 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=6HUF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HUF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6huf]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HUF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6HUF FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.82Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RAB27A, RAB27 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=6huf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6huf OCA], [http://pdbe.org/6huf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6huf RCSB], [http://www.ebi.ac.uk/pdbsum/6huf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6huf ProSAT]</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=6huf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6huf OCA], [https://pdbe.org/6huf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6huf RCSB], [https://www.ebi.ac.uk/pdbsum/6huf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6huf ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Disease == | | == Disease == |
| - | [[http://www.uniprot.org/uniprot/RB27A_HUMAN RB27A_HUMAN]] Griscelli syndrome type 2. The disease is caused by mutations affecting the gene represented in this entry. | + | [https://www.uniprot.org/uniprot/RB27A_HUMAN RB27A_HUMAN] Griscelli syndrome type 2. The disease is caused by mutations affecting the gene represented in this entry. |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RB27A_HUMAN RB27A_HUMAN]] Plays a role in cytotoxic granule exocytosis in lymphocytes. Required for both granule maturation and granule docking and priming at the immunologic synapse.<ref>PMID:18812475</ref> | + | [https://www.uniprot.org/uniprot/RB27A_HUMAN RB27A_HUMAN] Plays a role in cytotoxic granule exocytosis in lymphocytes. Required for both granule maturation and granule docking and priming at the immunologic synapse.<ref>PMID:18812475</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6huf" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6huf" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[GTP-binding protein 3D structures|GTP-binding protein 3D structures]] |
| | + | *[[Ras-related protein Rab 3D structures|Ras-related protein Rab 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Cota, E]] | + | [[Category: Cota E]] |
| - | [[Category: Jamshidiha, M]] | + | [[Category: Jamshidiha M]] |
| - | [[Category: Murray, J W]] | + | [[Category: Murray JW]] |
| - | [[Category: Perez-Dorado, I]] | + | [[Category: Perez-Dorado I]] |
| - | [[Category: Read, R J]] | + | [[Category: Read RJ]] |
| - | [[Category: Tate, E W]] | + | [[Category: Tate EW]] |
| - | [[Category: Exocytosis]]
| + | |
| - | [[Category: Gtpase]]
| + | |
| - | [[Category: Vesicle transport]]
| + | |
| Structural highlights
Disease
RB27A_HUMAN Griscelli syndrome type 2. The disease is caused by mutations affecting the gene represented in this entry.
Function
RB27A_HUMAN Plays a role in cytotoxic granule exocytosis in lymphocytes. Required for both granule maturation and granule docking and priming at the immunologic synapse.[1]
Publication Abstract from PubMed
Data pathologies caused by effects such as diffraction anisotropy and translational noncrystallographic symmetry (tNCS) can dramatically complicate the solution of the crystal structures of macromolecules. Such problems were encountered in determining the structure of a mutant form of Rab27a, a member of the Rab GTPases. Mutant Rab27a constructs that crystallize in the free form were designed for use in the discovery of drugs to reduce primary tumour invasiveness and metastasis. One construct, hRab27a(Mut), crystallized within 24 h and diffracted to 2.82 A resolution, with a unit cell possessing room for a large number of protein copies. Initial efforts to solve the structure using molecular replacement by Phaser were not successful. Analysis of the data set revealed that the crystals suffered from both extreme anisotropy and strong tNCS. As a result, large numbers of reflections had estimated standard deviations that were much larger than their measured intensities and their expected intensities, revealing problems with the use of such data at the time in Phaser. By eliminating extremely weak reflections with the largest combined effects of anisotropy and tNCS, these problems could be avoided, allowing a molecular-replacement solution to be found. The lessons that were learned in solving this structure have guided improvements in the numerical analysis used in Phaser, particularly in identifying diffraction measurements that convey very little information content. The calculation of information content could also be applied as an alternative to ellipsoidal truncation. The post-mortem analysis also revealed an oversight in accounting for measurement errors in the fast rotation function. While the crystal of mutant Rab27a is not amenable to drug screening, the structure can guide new modifications to obtain more suitable crystal forms.
Coping with strong translational noncrystallographic symmetry and extreme anisotropy in molecular replacement with Phaser: human Rab27a.,Jamshidiha M, Perez-Dorado I, Murray JW, Tate EW, Cota E, Read RJ Acta Crystallogr D Struct Biol. 2019 Mar 1;75(Pt 3):342-353. doi:, 10.1107/S2059798318017825. Epub 2019 Feb 28. PMID:30950405[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Menasche G, Menager MM, Lefebvre JM, Deutsch E, Athman R, Lambert N, Mahlaoui N, Court M, Garin J, Fischer A, de Saint Basile G. A newly identified isoform of Slp2a associates with Rab27a in cytotoxic T cells and participates to cytotoxic granule secretion. Blood. 2008 Dec 15;112(13):5052-62. doi: 10.1182/blood-2008-02-141069. Epub 2008 , Sep 23. PMID:18812475 doi:http://dx.doi.org/10.1182/blood-2008-02-141069
- ↑ Jamshidiha M, Perez-Dorado I, Murray JW, Tate EW, Cota E, Read RJ. Coping with strong translational noncrystallographic symmetry and extreme anisotropy in molecular replacement with Phaser: human Rab27a. Acta Crystallogr D Struct Biol. 2019 Mar 1;75(Pt 3):342-353. doi:, 10.1107/S2059798318017825. Epub 2019 Feb 28. PMID:30950405 doi:http://dx.doi.org/10.1107/S2059798318017825
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