1ulz: Difference between revisions

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

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

caption="1ulz, resolution 2.2Å" />

'''Crystal structure of the biotin carboxylase subunit of pyruvate carboxylase'''<br />

==Overview==

Pyruvate carboxylase (PC) is distributed in many eukaryotes as well as in, some prokaryotes. PC catalyzes the ATP-dependent carboxylation of pyruvate, to form oxalacetate. PC has three functional domains, one of which is a, biotin carboxylase (BC) domain. The BC subunit of PC from Aquifex aeolicus, (PC-beta) was crystallized in an orthorhombic form with space group, P2(1)2(1)2, unit-cell parameters a = 92.4, b = 122.1, c = 59.0 A and one, molecule in the asymmetric unit. Diffraction data were collected at 100 K, on BL24XU at SPring-8. The crystal structure was determined by the, molecular-replacement method and refined against 20.0-2.2 A resolution, data, giving an R factor of 0.199 and a free R factor of 0.236. The, crystal structure revealed that PC-beta forms a dimeric quaternary, structure consisting of two molecules related by crystallographic twofold, symmetry. The overall structure of PC-beta is similar to other, biotin-dependent carboxylases, such as acetyl-CoA carboxylase (ACC)., Although some parts of domain B were disordered in ACC, the corresponding, parts of PC-beta were clearly determined in the crystal structure. From, comparison between the active-site structure of ACC with ATP bound and a, virtual model of PC-beta with ATP bound, it was shown that the backbone, torsion angles of Glu203 in PC-beta change and some of water molecules in, the active site of PC-beta are excluded upon ATP binding.

Pyruvate carboxylase (PC) is distributed in many eukaryotes as well as in some prokaryotes. PC catalyzes the ATP-dependent carboxylation of pyruvate to form oxalacetate. PC has three functional domains, one of which is a biotin carboxylase (BC) domain. The BC subunit of PC from Aquifex aeolicus (PC-beta) was crystallized in an orthorhombic form with space group P2(1)2(1)2, unit-cell parameters a = 92.4, b = 122.1, c = 59.0 A and one molecule in the asymmetric unit. Diffraction data were collected at 100 K on BL24XU at SPring-8. The crystal structure was determined by the molecular-replacement method and refined against 20.0-2.2 A resolution data, giving an R factor of 0.199 and a free R factor of 0.236. The crystal structure revealed that PC-beta forms a dimeric quaternary structure consisting of two molecules related by crystallographic twofold symmetry. The overall structure of PC-beta is similar to other biotin-dependent carboxylases, such as acetyl-CoA carboxylase (ACC). Although some parts of domain B were disordered in ACC, the corresponding parts of PC-beta were clearly determined in the crystal structure. From comparison between the active-site structure of ACC with ATP bound and a virtual model of PC-beta with ATP bound, it was shown that the backbone torsion angles of Glu203 in PC-beta change and some of water molecules in the active site of PC-beta are excluded upon ATP binding.

==About this Structure==

1ULZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Active as [http://en.wikipedia.org/wiki/Pyruvate_carboxylase Pyruvate carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.4.1.1 6.4.1.1] Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1ULZ OCA].

1ULZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Active as [http://en.wikipedia.org/wiki/Pyruvate_carboxylase Pyruvate carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.4.1.1 6.4.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ULZ OCA].

==Reference==

Line 24:

[[Category: pyruvate carboxylase]]

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@@ Line 1: / Line 1: @@
-[[Image:1ulz.gif|left|200px]]<br /><applet load="1ulz" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1ulz.gif|left|200px]]<br /><applet load="1ulz" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1ulz, resolution 2.2&Aring;" />
 '''Crystal structure of the biotin carboxylase subunit of pyruvate carboxylase'''<br />
 ==Overview==
-Pyruvate carboxylase (PC) is distributed in many eukaryotes as well as in, some prokaryotes. PC catalyzes the ATP-dependent carboxylation of pyruvate, to form oxalacetate. PC has three functional domains, one of which is a, biotin carboxylase (BC) domain. The BC subunit of PC from Aquifex aeolicus, (PC-beta) was crystallized in an orthorhombic form with space group, P2(1)2(1)2, unit-cell parameters a = 92.4, b = 122.1, c = 59.0 A and one, molecule in the asymmetric unit. Diffraction data were collected at 100 K, on BL24XU at SPring-8. The crystal structure was determined by the, molecular-replacement method and refined against 20.0-2.2 A resolution, data, giving an R factor of 0.199 and a free R factor of 0.236. The, crystal structure revealed that PC-beta forms a dimeric quaternary, structure consisting of two molecules related by crystallographic twofold, symmetry. The overall structure of PC-beta is similar to other, biotin-dependent carboxylases, such as acetyl-CoA carboxylase (ACC)., Although some parts of domain B were disordered in ACC, the corresponding, parts of PC-beta were clearly determined in the crystal structure. From, comparison between the active-site structure of ACC with ATP bound and a, virtual model of PC-beta with ATP bound, it was shown that the backbone, torsion angles of Glu203 in PC-beta change and some of water molecules in, the active site of PC-beta are excluded upon ATP binding.
+Pyruvate carboxylase (PC) is distributed in many eukaryotes as well as in some prokaryotes. PC catalyzes the ATP-dependent carboxylation of pyruvate to form oxalacetate. PC has three functional domains, one of which is a biotin carboxylase (BC) domain. The BC subunit of PC from Aquifex aeolicus (PC-beta) was crystallized in an orthorhombic form with space group P2(1)2(1)2, unit-cell parameters a = 92.4, b = 122.1, c = 59.0 A and one molecule in the asymmetric unit. Diffraction data were collected at 100 K on BL24XU at SPring-8. The crystal structure was determined by the molecular-replacement method and refined against 20.0-2.2 A resolution data, giving an R factor of 0.199 and a free R factor of 0.236. The crystal structure revealed that PC-beta forms a dimeric quaternary structure consisting of two molecules related by crystallographic twofold symmetry. The overall structure of PC-beta is similar to other biotin-dependent carboxylases, such as acetyl-CoA carboxylase (ACC). Although some parts of domain B were disordered in ACC, the corresponding parts of PC-beta were clearly determined in the crystal structure. From comparison between the active-site structure of ACC with ATP bound and a virtual model of PC-beta with ATP bound, it was shown that the backbone torsion angles of Glu203 in PC-beta change and some of water molecules in the active site of PC-beta are excluded upon ATP binding.
 ==About this Structure==
-ULZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Active as [http://en.wikipedia.org/wiki/Pyruvate_carboxylase Pyruvate carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.4.1.1 6.4.1.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ULZ OCA].
+ULZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Active as [http://en.wikipedia.org/wiki/Pyruvate_carboxylase Pyruvate carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.4.1.1 6.4.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ULZ OCA].
 ==Reference==
@@ Line 24: / Line 24: @@
 [[Category: pyruvate carboxylase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 04:12:15 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:25:59 2008''