1jj7

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(New page: 200px<br /> <applet load="1jj7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jj7, resolution 2.40&Aring;" /> '''Crystal Structure o...)
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<applet load="1jj7" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1jj7, resolution 2.40&Aring;" />
caption="1jj7, resolution 2.40&Aring;" />
'''Crystal Structure of the C-terminal ATPase domain of human TAP1'''<br />
'''Crystal Structure of the C-terminal ATPase domain of human TAP1'''<br />
==Overview==
==Overview==
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The transporter associated with antigen processing (TAP) is an ABC, transporter formed of two subunits, TAP1 and TAP2, each of which has an, N-terminal membrane-spanning domain and a C-terminal ABC ATPase domain. We, report the structure of the C-terminal ABC ATPase domain of TAP1 (cTAP1), bound to ADP. cTAP1 forms an L-shaped molecule with two domains, a, RecA-like domain and a small alpha-helical domain. The diphosphate group, of ADP interacts with the P-loop as expected. Residues thought to be, involved in gamma-phosphate binding and hydrolysis show flexibility in the, ADP-bound state as evidenced by their high B-factors. Comparisons of cTAP1, with other ABC ATPases from the ABC transporter family as well as ABC, ATPases involved in DNA maintenance and repair reveal key regions and, residues specific to each family. Three ATPase subfamilies are identified, which have distinct adenosine recognition motifs, as well as distinct, subdomains that may be specific to the different functions of each, subfamily. Differences between TAP1 and TAP2 in the nucleotide-binding, site may be related to the observed asymmetry during peptide transport.
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The transporter associated with antigen processing (TAP) is an ABC transporter formed of two subunits, TAP1 and TAP2, each of which has an N-terminal membrane-spanning domain and a C-terminal ABC ATPase domain. We report the structure of the C-terminal ABC ATPase domain of TAP1 (cTAP1) bound to ADP. cTAP1 forms an L-shaped molecule with two domains, a RecA-like domain and a small alpha-helical domain. The diphosphate group of ADP interacts with the P-loop as expected. Residues thought to be involved in gamma-phosphate binding and hydrolysis show flexibility in the ADP-bound state as evidenced by their high B-factors. Comparisons of cTAP1 with other ABC ATPases from the ABC transporter family as well as ABC ATPases involved in DNA maintenance and repair reveal key regions and residues specific to each family. Three ATPase subfamilies are identified which have distinct adenosine recognition motifs, as well as distinct subdomains that may be specific to the different functions of each subfamily. Differences between TAP1 and TAP2 in the nucleotide-binding site may be related to the observed asymmetry during peptide transport.
==About this Structure==
==About this Structure==
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1JJ7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MG and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JJ7 OCA].
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1JJ7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JJ7 OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Gaudet, R.]]
[[Category: Gaudet, R.]]
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[[Category: Wiley, D.C.]]
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[[Category: Wiley, D C.]]
[[Category: ADP]]
[[Category: ADP]]
[[Category: MG]]
[[Category: MG]]
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[[Category: p-loop]]
[[Category: p-loop]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:41:08 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:23:19 2008''

Revision as of 11:23, 21 February 2008


1jj7, resolution 2.40Å

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Crystal Structure of the C-terminal ATPase domain of human TAP1

Overview

The transporter associated with antigen processing (TAP) is an ABC transporter formed of two subunits, TAP1 and TAP2, each of which has an N-terminal membrane-spanning domain and a C-terminal ABC ATPase domain. We report the structure of the C-terminal ABC ATPase domain of TAP1 (cTAP1) bound to ADP. cTAP1 forms an L-shaped molecule with two domains, a RecA-like domain and a small alpha-helical domain. The diphosphate group of ADP interacts with the P-loop as expected. Residues thought to be involved in gamma-phosphate binding and hydrolysis show flexibility in the ADP-bound state as evidenced by their high B-factors. Comparisons of cTAP1 with other ABC ATPases from the ABC transporter family as well as ABC ATPases involved in DNA maintenance and repair reveal key regions and residues specific to each family. Three ATPase subfamilies are identified which have distinct adenosine recognition motifs, as well as distinct subdomains that may be specific to the different functions of each subfamily. Differences between TAP1 and TAP2 in the nucleotide-binding site may be related to the observed asymmetry during peptide transport.

About this Structure

1JJ7 is a Single protein structure of sequence from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.

Reference

Structure of the ABC ATPase domain of human TAP1, the transporter associated with antigen processing., Gaudet R, Wiley DC, EMBO J. 2001 Sep 3;20(17):4964-72. PMID:11532960

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