1b7g

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1b7g" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b7g, resolution 2.05&Aring;" /> '''GLYCERALDEHYDE 3-PHO...)
Line 1: Line 1:
-
[[Image:1b7g.jpg|left|200px]]<br /><applet load="1b7g" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1b7g.jpg|left|200px]]<br /><applet load="1b7g" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1b7g, resolution 2.05&Aring;" />
caption="1b7g, resolution 2.05&Aring;" />
'''GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE'''<br />
'''GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE'''<br />
==Overview==
==Overview==
-
The enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from the, archaea shows low sequence identity (16-20%) with its eubacterial and, eukaryotic counterparts. The crystal structure of the apo GAPDH from, Sulfolobus solfataricus has been determined by multiple isomorphous, replacement at 2.05 A resolution. The enzyme has several differences in, secondary structure when compared with eubacterial GAPDHs, with an overall, increase in the number of alpha-helices. There is a relocation of the, active-site residues within the catalytic domain of the enzyme. The, thermostability of the S. solfataricus enzyme can be attributed to a, combination of an ion pair cluster and an intrasubunit disulphide bond.
+
The enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from the archaea shows low sequence identity (16-20%) with its eubacterial and eukaryotic counterparts. The crystal structure of the apo GAPDH from Sulfolobus solfataricus has been determined by multiple isomorphous replacement at 2.05 A resolution. The enzyme has several differences in secondary structure when compared with eubacterial GAPDHs, with an overall increase in the number of alpha-helices. There is a relocation of the active-site residues within the catalytic domain of the enzyme. The thermostability of the S. solfataricus enzyme can be attributed to a combination of an ion pair cluster and an intrasubunit disulphide bond.
==About this Structure==
==About this Structure==
-
1B7G is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glyceraldehyde-3-phosphate_dehydrogenase_(phosphorylating) Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.12 1.2.1.12] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1B7G OCA].
+
1B7G is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glyceraldehyde-3-phosphate_dehydrogenase_(phosphorylating) Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.12 1.2.1.12] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B7G OCA].
==Reference==
==Reference==
Line 14: Line 14:
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Sulfolobus solfataricus]]
[[Category: Sulfolobus solfataricus]]
-
[[Category: Isupov, M.N.]]
+
[[Category: Isupov, M N.]]
-
[[Category: Littlechild, J.A.]]
+
[[Category: Littlechild, J A.]]
[[Category: SO4]]
[[Category: SO4]]
[[Category: archaea; hyperthermophile; gapdh; hyperthermophilic dehydrogenase]]
[[Category: archaea; hyperthermophile; gapdh; hyperthermophilic dehydrogenase]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:25:42 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:52:20 2008''

Revision as of 09:52, 21 February 2008


1b7g, resolution 2.05Å

Drag the structure with the mouse to rotate

GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE

Overview

The enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from the archaea shows low sequence identity (16-20%) with its eubacterial and eukaryotic counterparts. The crystal structure of the apo GAPDH from Sulfolobus solfataricus has been determined by multiple isomorphous replacement at 2.05 A resolution. The enzyme has several differences in secondary structure when compared with eubacterial GAPDHs, with an overall increase in the number of alpha-helices. There is a relocation of the active-site residues within the catalytic domain of the enzyme. The thermostability of the S. solfataricus enzyme can be attributed to a combination of an ion pair cluster and an intrasubunit disulphide bond.

About this Structure

1B7G is a Single protein structure of sequence from Sulfolobus solfataricus with as ligand. Active as Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating), with EC number 1.2.1.12 Full crystallographic information is available from OCA.

Reference

Crystal structure of the glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeon Sulfolobus solfataricus., Isupov MN, Fleming TM, Dalby AR, Crowhurst GS, Bourne PC, Littlechild JA, J Mol Biol. 1999 Aug 20;291(3):651-60. PMID:10448043

Page seeded by OCA on Thu Feb 21 11:52:20 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools