Crystal structure of Rab9 complexed to GDP reveals a dimer with an active conformation of switch II
The small GTPase Rab9 is an essential regulator of vesicular transport from the late endosome to the trans-Golgi network, as monitored by the redirection of the mannose-6-phosphate receptors. The crystal structure of Rab9 complexed to GDP, Mg 2+, and Sr 2+ reveals a unique dimer formed by an intermo...
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| Veröffentlicht in: | FEBS letters 2004-06, Vol.568 (1), p.23-29 |
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| creator | Wittmann, Julia G Rudolph, Markus G |
| description | The small GTPase Rab9 is an essential regulator of vesicular transport from the late endosome to the trans-Golgi network, as monitored by the redirection of the mannose-6-phosphate receptors. The crystal structure of Rab9 complexed to GDP, Mg
2+, and Sr
2+ reveals a unique dimer formed by an intermolecular β-sheet that buries the switch I regions. Surface area and shape complementarity calculations suggest that Rab9 dimers can form an inactive, membrane-bound pool of Rab9
·
GDP that is independent of GDI. Mg
2+-bound Rab9 represents an inactive state, but Sr
2+-bound Rab9
·
GDP displays activated switch region conformations, mimicking those of the GTP state. A hydrophobic tetrad is formed resembling an effector-discriminating epitope found only in GTP-bound Rab proteins. |
| doi_str_mv | 10.1016/j.febslet.2004.05.004 |
| format | Article |
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2+, and Sr
2+ reveals a unique dimer formed by an intermolecular β-sheet that buries the switch I regions. Surface area and shape complementarity calculations suggest that Rab9 dimers can form an inactive, membrane-bound pool of Rab9
·
GDP that is independent of GDI. Mg
2+-bound Rab9 represents an inactive state, but Sr
2+-bound Rab9
·
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2+, and Sr
2+ reveals a unique dimer formed by an intermolecular β-sheet that buries the switch I regions. Surface area and shape complementarity calculations suggest that Rab9 dimers can form an inactive, membrane-bound pool of Rab9
·
GDP that is independent of GDI. Mg
2+-bound Rab9 represents an inactive state, but Sr
2+-bound Rab9
·
GDP displays activated switch region conformations, mimicking those of the GTP state. A hydrophobic tetrad is formed resembling an effector-discriminating epitope found only in GTP-bound Rab proteins.</description><subject>Amino Acid Sequence</subject><subject>CDR, complementary determining region</subject><subject>Crystal structure</subject><subject>Crystallography, X-Ray</subject><subject>Dimerization</subject><subject>GAP, GTPase activating protein</subject><subject>GDI, guanine nucleotide dissociation inhibitor</subject><subject>GEF, guanine nucleotide exchange factor</subject><subject>Guanosine Diphosphate - chemistry</subject><subject>Guanosine Diphosphate - metabolism</subject><subject>Intracellular transport</subject><subject>Merohedral twinning</subject><subject>Metals - chemistry</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>MPRs, mannose-6-phosphate receptors</subject><subject>Protein Conformation</subject><subject>Protein–protein interaction</subject><subject>rab GTP-Binding Proteins - chemistry</subject><subject>rab GTP-Binding Proteins - metabolism</subject><subject>Ras-like GTPase</subject><subject>REP, Rab escort protein</subject><subject>Sequence Homology, Amino Acid</subject><subject>TGN, trans-Golgi network</subject><subject>TIP47, tail interacting protein of 47 kDa</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNUctu2zAQJIoGjZv2E1rw1JsUkuJDOhWt8zIQIEEfZ4KiVggNSXRJyqn_vhRsoMfkNFjszOzuLEKfKCkpofJyW_bQxgFSyQjhJRFlhjdoRWtVFRWX9Vu0IoTyQqimOkfvY9ySXNe0eYfOqaCNbChfIbsOh5jMgGMKs01zAOx7_MO0DbZ-3A3wFzqcPL69esQB9mCGiA3u3AgBP7v0hM2EjU1uD5k_9T6MJjk_LSYx9-0T3mw-oLM-6-DjCS_Q75vrX-u74v7hdrP-dl9YziQruGFM5f2auuNdLxrV1X3dqFZYJZWQ1HIw-aDK8LqlFlgFnIBQnQRiZMNZdYG-HH13wf-ZISY9umhhGMwEfo5aMcK4ojITxZFog48xQK93wY0mHDQleklXb_UpXb2kq4nQGbLu82nA3I7Q_Ved4syEuyPh2Q1weJ2rvrn-zn4ur1o-RTghoqbLMV-PVpAT2zsIOloHk4XOBbBJd969sO0_xiuiag</recordid><startdate>20040618</startdate><enddate>20040618</enddate><creator>Wittmann, Julia G</creator><creator>Rudolph, Markus G</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20040618</creationdate><title>Crystal structure of Rab9 complexed to GDP reveals a dimer with an active conformation of switch II</title><author>Wittmann, Julia G ; Rudolph, Markus G</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4262-4a22781998d4df597d8f897b5c767561c4ea0143a48b1ce23e40e57d6e0a69423</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Amino Acid Sequence</topic><topic>CDR, complementary determining region</topic><topic>Crystal structure</topic><topic>Crystallography, X-Ray</topic><topic>Dimerization</topic><topic>GAP, GTPase activating protein</topic><topic>GDI, guanine nucleotide dissociation inhibitor</topic><topic>GEF, guanine nucleotide exchange factor</topic><topic>Guanosine Diphosphate - chemistry</topic><topic>Guanosine Diphosphate - metabolism</topic><topic>Intracellular transport</topic><topic>Merohedral twinning</topic><topic>Metals - chemistry</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>MPRs, mannose-6-phosphate receptors</topic><topic>Protein Conformation</topic><topic>Protein–protein interaction</topic><topic>rab GTP-Binding Proteins - chemistry</topic><topic>rab GTP-Binding Proteins - metabolism</topic><topic>Ras-like GTPase</topic><topic>REP, Rab escort protein</topic><topic>Sequence Homology, Amino Acid</topic><topic>TGN, trans-Golgi network</topic><topic>TIP47, tail interacting protein of 47 kDa</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wittmann, Julia G</creatorcontrib><creatorcontrib>Rudolph, Markus G</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wittmann, Julia G</au><au>Rudolph, Markus G</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystal structure of Rab9 complexed to GDP reveals a dimer with an active conformation of switch II</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2004-06-18</date><risdate>2004</risdate><volume>568</volume><issue>1</issue><spage>23</spage><epage>29</epage><pages>23-29</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>The small GTPase Rab9 is an essential regulator of vesicular transport from the late endosome to the trans-Golgi network, as monitored by the redirection of the mannose-6-phosphate receptors. The crystal structure of Rab9 complexed to GDP, Mg
2+, and Sr
2+ reveals a unique dimer formed by an intermolecular β-sheet that buries the switch I regions. Surface area and shape complementarity calculations suggest that Rab9 dimers can form an inactive, membrane-bound pool of Rab9
·
GDP that is independent of GDI. Mg
2+-bound Rab9 represents an inactive state, but Sr
2+-bound Rab9
·
GDP displays activated switch region conformations, mimicking those of the GTP state. A hydrophobic tetrad is formed resembling an effector-discriminating epitope found only in GTP-bound Rab proteins.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>15196914</pmid><doi>10.1016/j.febslet.2004.05.004</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
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| ispartof | FEBS letters, 2004-06, Vol.568 (1), p.23-29 |
| issn | 0014-5793 1873-3468 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_72024716 |
| source | MEDLINE; Elsevier ScienceDirect Journals Complete; Wiley Online Library Journals Frontfile Complete; Wiley Online Library Free Content; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence CDR, complementary determining region Crystal structure Crystallography, X-Ray Dimerization GAP, GTPase activating protein GDI, guanine nucleotide dissociation inhibitor GEF, guanine nucleotide exchange factor Guanosine Diphosphate - chemistry Guanosine Diphosphate - metabolism Intracellular transport Merohedral twinning Metals - chemistry Models, Molecular Molecular Sequence Data MPRs, mannose-6-phosphate receptors Protein Conformation Protein–protein interaction rab GTP-Binding Proteins - chemistry rab GTP-Binding Proteins - metabolism Ras-like GTPase REP, Rab escort protein Sequence Homology, Amino Acid TGN, trans-Golgi network TIP47, tail interacting protein of 47 kDa |
| title | Crystal structure of Rab9 complexed to GDP reveals a dimer with an active conformation of switch II |
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