2avf: Difference between revisions

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

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

caption="2avf, resolution 2.6Å" />

'''Crystal Structure of C-terminal Desundecapeptide Nitrite Reductase from Achromobacter cycloclastes'''<br />

==Overview==

Monoclinic crystal structure of C-terminal desundecapeptide nitrite, reductase (NiRc-11) from Achromobacter cycloclastes was determined at, 2.6A. NiRc-11 exists as a loose trimer in the crystal. Deletion of 11, residues eliminates all intersubunit hydrogen bonds mediated by the, C-terminal tail. The rigid irregular coil 105-112, which constitutes part, of the sidewall of the active site pocket, undergoes conformational, changes and becomes highly flexible in NiRc-11. Correspondingly, the, linker segments between the two copper sites 95-100 and 135-136 are partly, relaxed in conformation, which leads to disrupted active site, microenvironments responsible for the activity loss and spectral change of, NiRc-11. Comparison with the native structure revealed a bulky residue, Met331 fastened by hydrogen bonding, which may play a direct role in, keeping the right copper site geometry by protruding its side chain, against the irregular coil 105-112. Sequence alignment showed that the, bulky residue is conserved at position 331, indicating an equal importance, of C-terminal segment in other copper-containing nitrite reductases.

Monoclinic crystal structure of C-terminal desundecapeptide nitrite reductase (NiRc-11) from Achromobacter cycloclastes was determined at 2.6A. NiRc-11 exists as a loose trimer in the crystal. Deletion of 11 residues eliminates all intersubunit hydrogen bonds mediated by the C-terminal tail. The rigid irregular coil 105-112, which constitutes part of the sidewall of the active site pocket, undergoes conformational changes and becomes highly flexible in NiRc-11. Correspondingly, the linker segments between the two copper sites 95-100 and 135-136 are partly relaxed in conformation, which leads to disrupted active site microenvironments responsible for the activity loss and spectral change of NiRc-11. Comparison with the native structure revealed a bulky residue Met331 fastened by hydrogen bonding, which may play a direct role in keeping the right copper site geometry by protruding its side chain against the irregular coil 105-112. Sequence alignment showed that the bulky residue is conserved at position 331, indicating an equal importance of C-terminal segment in other copper-containing nitrite reductases.

==About this Structure==

2AVF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Achromobacter_cycloclastes Achromobacter cycloclastes] with CU and CL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Nitrite_reductase_(NO-forming) Nitrite reductase (NO-forming)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.2.1 1.7.2.1] Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=2AVF OCA].

2AVF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Achromobacter_cycloclastes Achromobacter cycloclastes] with <scene name='pdbligand=CU:'>CU</scene> and <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Nitrite_reductase_(NO-forming) Nitrite reductase (NO-forming)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.2.1 1.7.2.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AVF OCA].

==Reference==

Line 14:

[[Category: Nitrite reductase (NO-forming)]]

[[Category: Single protein]]

[[Category: An, X.M.]]

[[Category: An, X M.]]

[[Category: Chang, T.]]

[[Category: Chang, W.C.]]

[[Category: Chang, W C.]]

[[Category: Chang, W.R.]]

[[Category: Chang, W R.]]

[[Category: Chen, C.J.]]

[[Category: Chen, C J.]]

[[Category: Gui, L.L.]]

[[Category: Gui, L L.]]

[[Category: Li, H.T.]]

[[Category: Li, H T.]]

[[Category: Liu, M.Y.]]

[[Category: Liu, M Y.]]

[[Category: Zhang, J.P.]]

[[Category: Zhang, J P.]]

[[Category: CL]]

[[Category: CU]]

[[Category: beta barrel trimer]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 08:23~~:38 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:31:23 2008''

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@@ Line 1: / Line 1: @@
-[[Image:2avf.gif|left|200px]]<br /><applet load="2avf" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2avf.gif|left|200px]]<br /><applet load="2avf" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2avf, resolution 2.6&Aring;" />
 '''Crystal Structure of C-terminal Desundecapeptide Nitrite Reductase from Achromobacter cycloclastes'''<br />
 ==Overview==
-Monoclinic crystal structure of C-terminal desundecapeptide nitrite, reductase (NiRc-11) from Achromobacter cycloclastes was determined at, 2.6A. NiRc-11 exists as a loose trimer in the crystal. Deletion of 11, residues eliminates all intersubunit hydrogen bonds mediated by the, C-terminal tail. The rigid irregular coil 105-112, which constitutes part, of the sidewall of the active site pocket, undergoes conformational, changes and becomes highly flexible in NiRc-11. Correspondingly, the, linker segments between the two copper sites 95-100 and 135-136 are partly, relaxed in conformation, which leads to disrupted active site, microenvironments responsible for the activity loss and spectral change of, NiRc-11. Comparison with the native structure revealed a bulky residue, Met331 fastened by hydrogen bonding, which may play a direct role in, keeping the right copper site geometry by protruding its side chain, against the irregular coil 105-112. Sequence alignment showed that the, bulky residue is conserved at position 331, indicating an equal importance, of C-terminal segment in other copper-containing nitrite reductases.
+Monoclinic crystal structure of C-terminal desundecapeptide nitrite reductase (NiRc-11) from Achromobacter cycloclastes was determined at 2.6A. NiRc-11 exists as a loose trimer in the crystal. Deletion of 11 residues eliminates all intersubunit hydrogen bonds mediated by the C-terminal tail. The rigid irregular coil 105-112, which constitutes part of the sidewall of the active site pocket, undergoes conformational changes and becomes highly flexible in NiRc-11. Correspondingly, the linker segments between the two copper sites 95-100 and 135-136 are partly relaxed in conformation, which leads to disrupted active site microenvironments responsible for the activity loss and spectral change of NiRc-11. Comparison with the native structure revealed a bulky residue Met331 fastened by hydrogen bonding, which may play a direct role in keeping the right copper site geometry by protruding its side chain against the irregular coil 105-112. Sequence alignment showed that the bulky residue is conserved at position 331, indicating an equal importance of C-terminal segment in other copper-containing nitrite reductases.
 ==About this Structure==
-AVF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Achromobacter_cycloclastes Achromobacter cycloclastes] with CU and CL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Nitrite_reductase_(NO-forming) Nitrite reductase (NO-forming)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.2.1 1.7.2.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2AVF OCA].
+AVF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Achromobacter_cycloclastes Achromobacter cycloclastes] with <scene name='pdbligand=CU:'>CU</scene> and <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Nitrite_reductase_(NO-forming) Nitrite reductase (NO-forming)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.2.1 1.7.2.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AVF OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Nitrite reductase (NO-forming)]]
 [[Category: Single protein]]
-[[Category: An, X.M.]]
+[[Category: An, X M.]]
 [[Category: Chang, T.]]
-[[Category: Chang, W.C.]]
+[[Category: Chang, W C.]]
-[[Category: Chang, W.R.]]
+[[Category: Chang, W R.]]
-[[Category: Chen, C.J.]]
+[[Category: Chen, C J.]]
-[[Category: Gui, L.L.]]
+[[Category: Gui, L L.]]
-[[Category: Li, H.T.]]
+[[Category: Li, H T.]]
-[[Category: Liu, M.Y.]]
+[[Category: Liu, M Y.]]
-[[Category: Zhang, J.P.]]
+[[Category: Zhang, J P.]]
 [[Category: CL]]
 [[Category: CU]]
 [[Category: beta barrel trimer]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:23:38 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:31:23 2008''