1jlh
From Proteopedia
(New page: 200px<br /> <applet load="1jlh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jlh, resolution 2.10Å" /> '''Human Glucose-6-pho...) |
|||
Line 1: | Line 1: | ||
- | [[Image:1jlh.gif|left|200px]]<br /> | + | [[Image:1jlh.gif|left|200px]]<br /><applet load="1jlh" size="350" color="white" frame="true" align="right" spinBox="true" |
- | <applet load="1jlh" size=" | + | |
caption="1jlh, resolution 2.10Å" /> | caption="1jlh, resolution 2.10Å" /> | ||
'''Human Glucose-6-phosphate Isomerase'''<br /> | '''Human Glucose-6-phosphate Isomerase'''<br /> | ||
==Overview== | ==Overview== | ||
- | The second enzyme in the glycolytic pathway, phosphoglucose isomerase | + | The second enzyme in the glycolytic pathway, phosphoglucose isomerase (PGI), catalyses an intracellular aldose-ketose isomerization. Here we describe the human recombinant PGI structure (hPGI) solved in the absence of active site ligands. Crystals isomorphous to those previously reported were used to collect a 94% complete data set to a limiting resolution of 2.1 A. From the comparison between the free active site hPGI structure and the available human and rabbit PGI (rPGI) structures, a mechanism for protein initial catalytic steps is proposed. Binding of the phosphate moiety of the substrate to two distinct elements of the active site is responsible for driving a series of structural changes resulting in the polarisation of the active site histidine, priming it for the initial ring-opening step of catalysis. |
==Disease== | ==Disease== | ||
Line 11: | Line 10: | ||
==About this Structure== | ==About this Structure== | ||
- | 1JLH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Glucose-6-phosphate_isomerase Glucose-6-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.9 5.3.1.9] Full crystallographic information is available from [http:// | + | 1JLH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Glucose-6-phosphate_isomerase Glucose-6-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.9 5.3.1.9] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JLH OCA]. |
==Reference== | ==Reference== | ||
Line 18: | Line 17: | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
- | [[Category: Cordeiro, A | + | [[Category: Cordeiro, A T.]] |
[[Category: glycolysis]] | [[Category: glycolysis]] | ||
[[Category: glyconeogenesis]] | [[Category: glyconeogenesis]] | ||
[[Category: isomerase]] | [[Category: isomerase]] | ||
- | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:24:00 2008'' |
Revision as of 11:24, 21 February 2008
|
Human Glucose-6-phosphate Isomerase
Contents |
Overview
The second enzyme in the glycolytic pathway, phosphoglucose isomerase (PGI), catalyses an intracellular aldose-ketose isomerization. Here we describe the human recombinant PGI structure (hPGI) solved in the absence of active site ligands. Crystals isomorphous to those previously reported were used to collect a 94% complete data set to a limiting resolution of 2.1 A. From the comparison between the free active site hPGI structure and the available human and rabbit PGI (rPGI) structures, a mechanism for protein initial catalytic steps is proposed. Binding of the phosphate moiety of the substrate to two distinct elements of the active site is responsible for driving a series of structural changes resulting in the polarisation of the active site histidine, priming it for the initial ring-opening step of catalysis.
Disease
Known diseases associated with this structure: Hemolytic anemia due to glucosephosphate isomerase deficiency OMIM:[172400], Hydrops fetalis, one form OMIM:[172400]
About this Structure
1JLH is a Single protein structure of sequence from Homo sapiens. Active as Glucose-6-phosphate isomerase, with EC number 5.3.1.9 Full crystallographic information is available from OCA.
Reference
Crystal structure of human phosphoglucose isomerase and analysis of the initial catalytic steps., Cordeiro AT, Godoi PH, Silva CH, Garratt RC, Oliva G, Thiemann OH, Biochim Biophys Acta. 2003 Feb 21;1645(2):117-22. PMID:12573240
Page seeded by OCA on Thu Feb 21 13:24:00 2008