1oxu: Difference between revisions

Revision as of 16:27, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1oxu.png

Template:STRUCTURE 1oxu

Crystal structure of GlcV, the ABC-ATPase of the glucose ABC transporter from Sulfolobus solfataricusCrystal structure of GlcV, the ABC-ATPase of the glucose ABC transporter from Sulfolobus solfataricus

Template:ABSTRACT PUBMED 12823973

About this StructureAbout this Structure

1OXU is a Single protein structure of sequence from Sulfolobus solfataricus. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structures of the ATPase subunit of the glucose ABC transporter from Sulfolobus solfataricus: nucleotide-free and nucleotide-bound conformations., Verdon G, Albers SV, Dijkstra BW, Driessen AJ, Thunnissen AM, J Mol Biol. 2003 Jul 4;330(2):343-58. PMID:12823973

Page seeded by OCA on Sun Jul 27 16:27:19 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1oxu.jpg|left|200px]]
+{{Seed}}
+[[Image:1oxu.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1oxu|  PDB=1oxu  |  SCENE=  }}
-'''Crystal structure of GlcV, the ABC-ATPase of the glucose ABC transporter from Sulfolobus solfataricus'''
+===Crystal structure of GlcV, the ABC-ATPase of the glucose ABC transporter from Sulfolobus solfataricus===
-==Overview==
+<!--
-The ABC-ATPase GlcV energizes a binding protein-dependent ABC transporter that mediates glucose uptake in Sulfolobus solfataricus. Here, we report high-resolution crystal structures of GlcV in different states along its catalytic cycle: distinct monomeric nucleotide-free states and monomeric complexes with ADP-Mg(2+) as a product-bound state, and with AMPPNP-Mg(2+) as an ATP-like bound state. The structure of GlcV consists of a typical ABC-ATPase domain, comprising two subdomains, connected by a linker region to a C-terminal domain of unknown function. Comparisons of the nucleotide-free and nucleotide-bound structures of GlcV reveal re-orientations of the ABCalpha subdomain and the C-terminal domain relative to the ABCalpha/beta subdomain, and switch-like rearrangements in the P-loop and Q-loop regions. Additionally, large conformational differences are observed between the GlcV structures and those of other ABC-ATPases, further emphasizing the inherent flexibility of these proteins. Notably, a comparison of the monomeric AMPPNP-Mg(2+)-bound GlcV structure with that of the dimeric ATP-Na(+)-bound LolD-E171Q mutant reveals a +/-20 degrees rigid body re-orientation of the ABCalpha subdomain relative to the ABCalpha/beta subdomain, accompanied by a local conformational difference in the Q-loop. We propose that these differences represent conformational changes that may have a role in the mechanism of energy-transduction and/or allosteric control of the ABC-ATPase activity in bacterial importers.
+The line below this paragraph, {{ABSTRACT_PUBMED_12823973}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12823973 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12823973}}
 ==About this Structure==
@@ Line 32: / Line 36: @@
 [[Category: Glcv]]
 [[Category: Sulfolobus solfataricus]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 04:24:41 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 16:27:19 2008''