2rji
From Proteopedia
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|PDB= 2rji |SIZE=350|CAPTION= <scene name='initialview01'>2rji</scene>, resolution 1.80Å | |PDB= 2rji |SIZE=350|CAPTION= <scene name='initialview01'>2rji</scene>, resolution 1.80Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= eba175reVIsynth ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5833 Plasmodium falciparum]) | |GENE= eba175reVIsynth ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5833 Plasmodium falciparum]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1sb0|1sb0]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2rji FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rji OCA], [http://www.ebi.ac.uk/pdbsum/2rji PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2rji RCSB]</span> | ||
}} | }} | ||
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[[Category: Blackman, M J.]] | [[Category: Blackman, M J.]] | ||
[[Category: Withers-Martinez, C.]] | [[Category: Withers-Martinez, C.]] | ||
| - | [[Category: CA]] | ||
[[Category: cbp kix]] | [[Category: cbp kix]] | ||
[[Category: cell invasion]] | [[Category: cell invasion]] | ||
| Line 32: | Line 34: | ||
[[Category: region vi]] | [[Category: region vi]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:01:09 2008'' |
Revision as of 02:01, 31 March 2008
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| , resolution 1.80Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | eba175reVIsynth (Plasmodium falciparum) | ||||||
| Related: | 1sb0
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Malarial EBA-175 region VI crystallographic structure reveals a KIX-like binding interface
Overview
The malaria parasite proliferates in the bloodstream of its vertebrate host by invading and replicating within erythrocytes. To achieve successful invasion, a number of discrete and essential events need to take place at the parasite-host cell interface. Erythrocyte-binding antigen 175 (EBA-175) is a member of a family of Plasmodium falciparum erythrocyte-binding proteins involved in the formation of a tight junction, a necessary step in invasion. Here we present the crystal structure of EBA-175 region VI (rVI), a cysteine-rich domain that is highly conserved within the protein family and is essential for EBA-175 trafficking. The structure was solved by selenomethionine single-wavelength anomalous dispersion at 1.8 A resolution. It reveals a homodimer, containing in each subunit a compact five-alpha-helix core that is stabilized by four conserved disulfide bridges. rVI adopts a novel fold that is likely conserved across the protein family, indicating a conserved function. It shows no similarity to the Duffy-binding-like domains of EBA-175 involved in erythrocyte binding, indicating a distinct role. Remarkably, rVI possesses structural features related to the KIX-binding domain of the coactivator CREB-binding protein, supporting the binding and trafficking roles that have been ascribed to it and providing a rational basis for further experimental investigation of its function.
About this Structure
2RJI is a Single protein structure of sequence from Plasmodium falciparum. Full crystallographic information is available from OCA.
Reference
Malarial EBA-175 region VI crystallographic structure reveals a KIX-like binding interface., Withers-Martinez C, Haire LF, Hackett F, Walker PA, Howell SA, Smerdon SJ, Dodson GG, Blackman MJ, J Mol Biol. 2008 Jan 18;375(3):773-81. Epub 2007 Nov 1. PMID:18036613
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