1rc2: Difference between revisions

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[[Image:1rc2.gif|left|200px]]<br /><applet load="1rc2" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1rc2.gif|left|200px]]<br /><applet load="1rc2" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1rc2, resolution 2.5Å" />

'''2.5 Angstrom Resolution X-ray Structure of Aquaporin Z'''<br />

==Overview==

Aquaporins are a family of water and small molecule channels found in, organisms ranging from bacteria to animals. One of these channels, the E., coli protein aquaporin Z (AqpZ), has been shown to selectively conduct, only water at high rates. We have expressed, purified, crystallized, and, solved the X-ray structure of AqpZ. The 2.5 A resolution structure of AqpZ, suggests aquaporin selectivity results both from a steric mechanism due to, pore size and from specific amino acid substitutions that regulate the, preference for a hydrophobic or hydrophilic substrate. This structure, provides direct evidence on the molecular mechanisms of specificity, between water and glycerol in this family of channels from a single, species. It is to our knowledge the first atomic resolution structure of a, recombinant aquaporin and so provides a platform for combined genetic, mutational, functional, and structural determinations of the mechanisms of, aquaporins and, more generally, the assembly of multimeric membrane, proteins.

Aquaporins are a family of water and small molecule channels found in organisms ranging from bacteria to animals. One of these channels, the E. coli protein aquaporin Z (AqpZ), has been shown to selectively conduct only water at high rates. We have expressed, purified, crystallized, and solved the X-ray structure of AqpZ. The 2.5 A resolution structure of AqpZ suggests aquaporin selectivity results both from a steric mechanism due to pore size and from specific amino acid substitutions that regulate the preference for a hydrophobic or hydrophilic substrate. This structure provides direct evidence on the molecular mechanisms of specificity between water and glycerol in this family of channels from a single species. It is to our knowledge the first atomic resolution structure of a recombinant aquaporin and so provides a platform for combined genetic, mutational, functional, and structural determinations of the mechanisms of aquaporins and, more generally, the assembly of multimeric membrane proteins.

==About this Structure==

1RC2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with BGL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1RC2 OCA].

1RC2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=BGL:'>BGL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RC2 OCA].

==Reference==

Line 13:

[[Category: Escherichia coli]]

[[Category: Single protein]]

[[Category: Egea, P.F.]]

[[Category: Egea, P F.]]

[[Category: III, J.D.O.Connell.]]

[[Category: III, J D.O Connell.]]

[[Category: Robles, Y.C.]]

[[Category: Robles, Y C.]]

[[Category: Savage, D.F.]]

[[Category: Savage, D F.]]

[[Category: Stroud, R.M.]]

[[Category: Stroud, R M.]]

[[Category: BGL]]

[[Category: aquaporin]]

[[Category: membrane protein]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 01:27:~~04 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:49:16 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1rc2.gif|left|200px]]<br /><applet load="1rc2" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1rc2.gif|left|200px]]<br /><applet load="1rc2" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1rc2, resolution 2.5&Aring;" />
 '''2.5 Angstrom Resolution X-ray Structure of Aquaporin Z'''<br />
 ==Overview==
-Aquaporins are a family of water and small molecule channels found in, organisms ranging from bacteria to animals. One of these channels, the E., coli protein aquaporin Z (AqpZ), has been shown to selectively conduct, only water at high rates. We have expressed, purified, crystallized, and, solved the X-ray structure of AqpZ. The 2.5 A resolution structure of AqpZ, suggests aquaporin selectivity results both from a steric mechanism due to, pore size and from specific amino acid substitutions that regulate the, preference for a hydrophobic or hydrophilic substrate. This structure, provides direct evidence on the molecular mechanisms of specificity, between water and glycerol in this family of channels from a single, species. It is to our knowledge the first atomic resolution structure of a, recombinant aquaporin and so provides a platform for combined genetic, mutational, functional, and structural determinations of the mechanisms of, aquaporins and, more generally, the assembly of multimeric membrane, proteins.
+Aquaporins are a family of water and small molecule channels found in organisms ranging from bacteria to animals. One of these channels, the E. coli protein aquaporin Z (AqpZ), has been shown to selectively conduct only water at high rates. We have expressed, purified, crystallized, and solved the X-ray structure of AqpZ. The 2.5 A resolution structure of AqpZ suggests aquaporin selectivity results both from a steric mechanism due to pore size and from specific amino acid substitutions that regulate the preference for a hydrophobic or hydrophilic substrate. This structure provides direct evidence on the molecular mechanisms of specificity between water and glycerol in this family of channels from a single species. It is to our knowledge the first atomic resolution structure of a recombinant aquaporin and so provides a platform for combined genetic, mutational, functional, and structural determinations of the mechanisms of aquaporins and, more generally, the assembly of multimeric membrane proteins.
 ==About this Structure==
-RC2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with BGL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RC2 OCA].
+RC2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=BGL:'>BGL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RC2 OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Escherichia coli]]
 [[Category: Single protein]]
-[[Category: Egea, P.F.]]
+[[Category: Egea, P F.]]
-[[Category: III, J.D.O.Connell.]]
+[[Category: III, J D.O Connell.]]
-[[Category: Robles, Y.C.]]
+[[Category: Robles, Y C.]]
-[[Category: Savage, D.F.]]
+[[Category: Savage, D F.]]
-[[Category: Stroud, R.M.]]
+[[Category: Stroud, R M.]]
 [[Category: BGL]]
 [[Category: aquaporin]]
 [[Category: membrane protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:27:04 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:49:16 2008''