PDBsum entry 1vci

Transport protein

PDB id

1vci

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Contents

			Protein chain

					353 a.a. *

			Ligands

					ATP

			Waters ×86

* Residue conservation analysis

PDB id:

1vci

Links

Name:

Transport protein

Title:

Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp

Structure:

Sugar-binding transport atp-binding protein. Chain: a. Synonym: atp binding cassette transporters, abc transporters. Engineered: yes

Source:

Pyrococcus horikoshii. Organism_taxid: 53953. Gene: ph0022. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.

Biol. unit:

Dimer (from PDB file)

Resolution:

2.90Å

R-factor:

0.215

R-free:

0.297

Authors:

T.Ose,T.Fujie,M.Yao,N.Watanabe,I.Tanaka

Key ref:

T.Ose et al. (2004). Crystal structure of the ATP-binding cassette of multisugar transporter from Pyrococcus horikoshii OT3. Proteins, 57, 635-638. PubMed id: 15382245 DOI: 10.1002/prot.20206

Date:

08-Mar-04

Release date:

14-Dec-04

PROCHECK

	Headers

	References

Protein chain

O57758 (O57758_PYRHO) - 373aa long hypothetical sugar-binding transport ATP-binding protein from Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)

Seq: Struc:					373 a.a. 353 a.a.

Key:

PfamA domain

Secondary structure

CATH domain



		Enzyme reactions

Enzyme class:

E.C.?

[IntEnz] [ExPASy] [KEGG] [BRENDA]

DOI no: 10.1002/prot.20206	Proteins 57:635-638 (2004)
PubMed id: 15382245

Crystal structure of the ATP-binding cassette of multisugar transporter from Pyrococcus horikoshii OT3.
T.Ose, T.Fujie, M.Yao, N.Watanabe, I.Tanaka.

ABSTRACT

No abstract given.

Selected figure(s)



	Figure 1. Figure 1. Crystal structure of PH0022. (a) Ribbon diagram of Pyrococcus horikoshii PH0022 protomer structure color-coded as Rec-A-like subdomain (blue), -helical subdomain (yellow), and RD (magenta). (b) Dimer structure of ATP-bound form. The ATP is shown in a ball-and-stick model, and the atoms are colored as follows: oxygen (red), nitrogen (blue), carbon (yellow), and phosphorus (magenta). (c) Top view of the superposition of the C -trace between PH0022 and E.c.MalK. The NBD and RD of PH0022 are colored yellow and red, respectively; the NBD and RD of E.c.MalK are colored light-blue and dark-blue, respectively. (d) Front view of the superposition of the C -trace between PH0022 and E.c.MalK. Each domain is colored the same as (c).		Figure 2. Figure 2. Stereo view of the electron density (2.1 contour level) at the active site of NBD of one of the AB homodimers from the F[o]-F[c] map. The refined ATP molecule (shown in a magenta ball-and-stick model) was omitted in the structure factor calculation. The residues that interact with the , , and phosphate groups of ATP are also shown in a gray ball-and-stick model. The atoms are colored as follows: oxygen (red), nitrogen (blue), carbon (yellow), sulfate (green), and phosphorus (magenta).

Literature references that cite this PDB file's key reference

PubMed id

Reference

20823549

M.Haffke, A.Menzel, Y.Carius, D.Jahn, and D.W.Heinz (2010).
Structures of the nucleotide-binding domain of the human ABCB6 transporter and its complexes with nucleotides.

Acta Crystallogr D Biol Crystallogr, 66, 979-987.

PDB codes:

3nh6 3nh9 3nha 3nhb

18540059

A.S.Ethayathulla, Y.Bessho, A.Shinkai, B.Padmanabhan, T.P.Singh, P.Kaur, and S.Yokoyama (2008).
Purification, crystallization and preliminary X-ray diffraction analysis of the putative ABC transporter ATP-binding protein from Thermotoga maritima.

Acta Crystallogr Sect F Struct Biol Cryst Commun, 64, 498-500.

17951296

J.Weng, J.Ma, K.Fan, and W.Wang (2008).
The conformational coupling and translocation mechanism of vitamin B12 ATP-binding cassette transporter BtuCD.

Biophys J, 94, 612-621.

18790847

P.C.Wen, and E.Tajkhorshid (2008).
Dimer opening of the nucleotide binding domains of ABC transporters after ATP hydrolysis.

Biophys J, 95, 5100-5110.

17485460

P.M.Jones, and A.M.George (2007).
Nucleotide-dependent allostery within the ABC transporter ATP-binding cassette: a computational study of the MJ0796 dimer.

J Biol Chem, 282, 22793-22803.

16541253

C.Oswald, I.B.Holland, and L.Schmitt (2006).
The motor domains of ABC-transporters. What can structures tell us?

Naunyn Schmiedebergs Arch Pharmacol, 372, 385-399.

16326809

G.Lu, J.M.Westbrooks, A.L.Davidson, and J.Chen (2005).
ATP hydrolysis is required to reset the ATP-binding cassette dimer into the resting-state conformation.

Proc Natl Acad Sci U S A, 102, 17969-17974.

PDB codes:

2awn 2awo

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.