2bov
From Proteopedia
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| - | [[Image:2bov.gif|left|200px]] | + | [[Image:2bov.gif|left|200px]] |
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| - | '''MOLECULAR RECOGNITION OF AN ADP-RIBOSYLATING CLOSTRIDIUM BOTULINUM C3 EXOENZYME BY RALA GTPASE''' | + | {{Structure |
| + | |PDB= 2bov |SIZE=350|CAPTION= <scene name='initialview01'>2bov</scene>, resolution 2.66Å | ||
| + | |SITE= <scene name='pdbsite=AC1:Mg+Binding+Site+For+Chain+A'>AC1</scene> | ||
| + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=GDP:GUANOSINE-5'-DIPHOSPHATE'>GDP</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''MOLECULAR RECOGNITION OF AN ADP-RIBOSYLATING CLOSTRIDIUM BOTULINUM C3 EXOENZYME BY RALA GTPASE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2BOV is a [ | + | 2BOV is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Clostridium_botulinum Clostridium botulinum] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry 1WCA. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BOV OCA]. |
==Reference== | ==Reference== | ||
| - | Molecular recognition of an ADP-ribosylating Clostridium botulinum C3 exoenzyme by RalA GTPase., Holbourn KP, Sutton JM, Evans HR, Shone CC, Acharya KR, Proc Natl Acad Sci U S A. 2005 Apr 12;102(15):5357-62. Epub 2005 Apr 4. PMID:[http:// | + | Molecular recognition of an ADP-ribosylating Clostridium botulinum C3 exoenzyme by RalA GTPase., Holbourn KP, Sutton JM, Evans HR, Shone CC, Acharya KR, Proc Natl Acad Sci U S A. 2005 Apr 12;102(15):5357-62. Epub 2005 Apr 4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15809419 15809419] |
[[Category: Clostridium botulinum]] | [[Category: Clostridium botulinum]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:04:43 2008'' |
Revision as of 14:04, 20 March 2008
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| , resolution 2.66Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
MOLECULAR RECOGNITION OF AN ADP-RIBOSYLATING CLOSTRIDIUM BOTULINUM C3 EXOENZYME BY RALA GTPASE
Overview
C3 exoenzymes (members of the ADP-ribosyltranferase family) are produced by Clostridium botulinum (C3bot1 and -2), Clostridium limosum (C3lim), Bacillus cereus (C3cer), and Staphylococcus aureus (C3stau1-3). These exoenzymes lack a translocation domain but are known to specifically inactivate Rho GTPases in host target cells. Here, we report the crystal structure of C3bot1 in complex with RalA (a GTPase of the Ras subfamily) and GDP at a resolution of 2.66 A. RalA is not ADP-ribosylated by C3 exoenzymes but inhibits ADP-ribosylation of RhoA by C3bot1, C3lim, and C3cer to different extents. The structure provides an insight into the molecular interactions between C3bot1 and RalA involving the catalytic ADP-ribosylating turn-turn (ARTT) loop from C3bot1 and helix alpha4 and strand beta6 (which are not part of the GDP-binding pocket) from RalA. The structure also suggests a molecular explanation for the different levels of C3-exoenzyme inhibition by RalA and why RhoA does not bind C3bot1 in this manner.
About this Structure
2BOV is a Protein complex structure of sequences from Clostridium botulinum and Homo sapiens. This structure supersedes the now removed PDB entry 1WCA. Full crystallographic information is available from OCA.
Reference
Molecular recognition of an ADP-ribosylating Clostridium botulinum C3 exoenzyme by RalA GTPase., Holbourn KP, Sutton JM, Evans HR, Shone CC, Acharya KR, Proc Natl Acad Sci U S A. 2005 Apr 12;102(15):5357-62. Epub 2005 Apr 4. PMID:15809419
Page seeded by OCA on Thu Mar 20 16:04:43 2008
Categories: Clostridium botulinum | Homo sapiens | Protein complex | Acharya, K R. | Evans, H R. | Holbourn, K P. | Shone, C C. | Sutton, J M. | GDP | MG | Adp | C3bot | Exoenzyme | Glycosyltransferase | Gtp-binding | Gtpase | Lipoprotein | Nad | Prenylation | Rala | Ribosylating toxin | Transferase
