2nq2: Difference between revisions

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[[Image:2nq2.gif|left|200px]]<br /><applet load="2nq2" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:2nq2.gif|left|200px]]<br /><applet load="2nq2" size="350" color="white" frame="true" align="right" spinBox="true"

caption="2nq2, resolution 2.400Å" />

'''An inward-facing conformation of a putative metal-chelate type ABC transporter.'''<br />

==Overview==

The crystal structure of a putative metal-chelate-type adenosine, triphosphate (ATP)-binding cassette (ABC) transporter encoded by genes, HI1470 and HI1471 of Haemophilus influenzae has been solved at 2.4, angstrom resolution. The permeation pathway exhibits an inward-facing, conformation, in contrast to the outward-facing state previously observed, for the homologous vitamin B12 importer BtuCD. Although the structures of, both HI1470/1 and BtuCD have been solved in nucleotide-free states, the, pairs of ABC subunits in these two structures differ by a translational, shift in the plane of the membrane that coincides with a repositioning of, the membrane-spanning subunits. The differences observed between these ABC, transporters involve relatively modest rearrangements and may serve as, structural models for inward- and outward-facing conformations relevant to, the alternating access mechanism of substrate translocation.

The crystal structure of a putative metal-chelate-type adenosine triphosphate (ATP)-binding cassette (ABC) transporter encoded by genes HI1470 and HI1471 of Haemophilus influenzae has been solved at 2.4 angstrom resolution. The permeation pathway exhibits an inward-facing conformation, in contrast to the outward-facing state previously observed for the homologous vitamin B12 importer BtuCD. Although the structures of both HI1470/1 and BtuCD have been solved in nucleotide-free states, the pairs of ABC subunits in these two structures differ by a translational shift in the plane of the membrane that coincides with a repositioning of the membrane-spanning subunits. The differences observed between these ABC transporters involve relatively modest rearrangements and may serve as structural models for inward- and outward-facing conformations relevant to the alternating access mechanism of substrate translocation.

==About this Structure==

2NQ2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=2NQ2 OCA].

2NQ2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NQ2 OCA].

==Reference==

Line 13:

[[Category: Haemophilus influenzae]]

[[Category: Protein complex]]

[[Category: Lee, A.T.]]

[[Category: Lee, A T.]]

[[Category: Locher, K.P.]]

[[Category: Locher, K P.]]

[[Category: Lum, P.]]

[[Category: Pinkett, H.P.]]

[[Category: Pinkett, H P.]]

[[Category: Rees, D.C.]]

[[Category: Rees, D C.]]

[[Category: atp-binding protein]]

[[Category: nucleotide binding domain]]

Line 23:

[[Category: transmembrane domain]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 12:50:~~32 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:09:39 2008''

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@@ Line 1: / Line 1: @@
-[[Image:2nq2.gif|left|200px]]<br /><applet load="2nq2" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2nq2.gif|left|200px]]<br /><applet load="2nq2" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2nq2, resolution 2.400&Aring;" />
 '''An inward-facing conformation of a putative metal-chelate type ABC transporter.'''<br />
 ==Overview==
-The crystal structure of a putative metal-chelate-type adenosine, triphosphate (ATP)-binding cassette (ABC) transporter encoded by genes, HI1470 and HI1471 of Haemophilus influenzae has been solved at 2.4, angstrom resolution. The permeation pathway exhibits an inward-facing, conformation, in contrast to the outward-facing state previously observed, for the homologous vitamin B12 importer BtuCD. Although the structures of, both HI1470/1 and BtuCD have been solved in nucleotide-free states, the, pairs of ABC subunits in these two structures differ by a translational, shift in the plane of the membrane that coincides with a repositioning of, the membrane-spanning subunits. The differences observed between these ABC, transporters involve relatively modest rearrangements and may serve as, structural models for inward- and outward-facing conformations relevant to, the alternating access mechanism of substrate translocation.
+The crystal structure of a putative metal-chelate-type adenosine triphosphate (ATP)-binding cassette (ABC) transporter encoded by genes HI1470 and HI1471 of Haemophilus influenzae has been solved at 2.4 angstrom resolution. The permeation pathway exhibits an inward-facing conformation, in contrast to the outward-facing state previously observed for the homologous vitamin B12 importer BtuCD. Although the structures of both HI1470/1 and BtuCD have been solved in nucleotide-free states, the pairs of ABC subunits in these two structures differ by a translational shift in the plane of the membrane that coincides with a repositioning of the membrane-spanning subunits. The differences observed between these ABC transporters involve relatively modest rearrangements and may serve as structural models for inward- and outward-facing conformations relevant to the alternating access mechanism of substrate translocation.
 ==About this Structure==
-NQ2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2NQ2 OCA].
+NQ2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NQ2 OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Haemophilus influenzae]]
 [[Category: Protein complex]]
-[[Category: Lee, A.T.]]
+[[Category: Lee, A T.]]
-[[Category: Locher, K.P.]]
+[[Category: Locher, K P.]]
 [[Category: Lum, P.]]
-[[Category: Pinkett, H.P.]]
+[[Category: Pinkett, H P.]]
-[[Category: Rees, D.C.]]
+[[Category: Rees, D C.]]
 [[Category: atp-binding protein]]
 [[Category: nucleotide binding domain]]
@@ Line 23: / Line 23: @@
 [[Category: transmembrane domain]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 12:50:32 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:09:39 2008''