1jlh: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
(13 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1jlh.gif|left|200px]]
<!--
The line below this paragraph, containing "STRUCTURE_1jlh", creates the "Structure Box" on the page.
You may change the PDB parameter (which sets the PDB file loaded into the applet)
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
or leave the SCENE parameter empty for the default display.
-->
{{STRUCTURE_1jlh|  PDB=1jlh  |  SCENE=  }}
'''Human Glucose-6-phosphate Isomerase'''


==Human Glucose-6-phosphate Isomerase==
<StructureSection load='1jlh' size='340' side='right'caption='[[1jlh]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1jlh]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JLH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JLH FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jlh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jlh OCA], [https://pdbe.org/1jlh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jlh RCSB], [https://www.ebi.ac.uk/pdbsum/1jlh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jlh ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/G6PI_HUMAN G6PI_HUMAN] Defects in GPI are the cause of hemolytic anemia non-spherocytic due to glucose phosphate isomerase deficiency (HA-GPID) [MIM:[https://omim.org/entry/613470 613470]. It is a form of anemia in which there is no abnormal hemoglobin or spherocytosis. It is caused by glucose phosphate isomerase deficiency. Severe GPI deficiency can be associated with hydrops fetalis, immediate neonatal death and neurological impairment.
== Function ==
[https://www.uniprot.org/uniprot/G6PI_HUMAN G6PI_HUMAN] Besides it's role as a glycolytic enzyme, mammalian GPI can function as a tumor-secreted cytokine and an angiogenic factor (AMF) that stimulates endothelial cell motility. GPI is also a neurotrophic factor (Neuroleukin) for spinal and sensory neurons.<ref>PMID:11004567</ref> <ref>PMID:11437381</ref> <ref>PMID:12163179</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jl/1jlh_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1jlh ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==Overview==
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<ref>PMID:12573240</ref>
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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1JLH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JLH OCA].
</div>
<div class="pdbe-citations 1jlh" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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:[http://www.ncbi.nlm.nih.gov/pubmed/12573240 12573240]
*[[Phosphoglucose isomerase 3D structures|Phosphoglucose isomerase 3D structures]]
[[Category: Glucose-6-phosphate isomerase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Cordeiro, A T.]]
[[Category: Cordeiro AT]]
[[Category: Glycolysis]]
[[Category: Glyconeogenesis]]
[[Category: Isomerase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 21:22:11 2008''

Latest revision as of 11:42, 16 August 2023

Human Glucose-6-phosphate IsomeraseHuman Glucose-6-phosphate Isomerase

Structural highlights

1jlh is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.1Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

G6PI_HUMAN Defects in GPI are the cause of hemolytic anemia non-spherocytic due to glucose phosphate isomerase deficiency (HA-GPID) [MIM:613470. It is a form of anemia in which there is no abnormal hemoglobin or spherocytosis. It is caused by glucose phosphate isomerase deficiency. Severe GPI deficiency can be associated with hydrops fetalis, immediate neonatal death and neurological impairment.

Function

G6PI_HUMAN Besides it's role as a glycolytic enzyme, mammalian GPI can function as a tumor-secreted cytokine and an angiogenic factor (AMF) that stimulates endothelial cell motility. GPI is also a neurotrophic factor (Neuroleukin) for spinal and sensory neurons.[1] [2] [3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Haga A, Niinaka Y, Raz A. Phosphohexose isomerase/autocrine motility factor/neuroleukin/maturation factor is a multifunctional phosphoprotein. Biochim Biophys Acta. 2000 Jul 14;1480(1-2):235-44. PMID:11004567
  2. ↑ Funasaka T, Haga A, Raz A, Nagase H. Tumor autocrine motility factor is an angiogenic factor that stimulates endothelial cell motility. Biochem Biophys Res Commun. 2001 Jul 6;285(1):118-28. PMID:11437381 doi:10.1006/bbrc.2001.5135
  3. ↑ Amraei M, Nabi IR. Species specificity of the cytokine function of phosphoglucose isomerase. FEBS Lett. 2002 Aug 14;525(1-3):151-5. PMID:12163179
  4. ↑ Cordeiro AT, Godoi PH, Silva CH, Garratt RC, Oliva G, Thiemann OH. Crystal structure of human phosphoglucose isomerase and analysis of the initial catalytic steps. Biochim Biophys Acta. 2003 Feb 21;1645(2):117-22. PMID:12573240

1jlh, resolution 2.10Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=1jlh&oldid=3828405"