2h5g: Difference between revisions

Latest revision as of 08:06, 30 October 2024

Crystal structure of human pyrroline-5-carboxylate synthetase

Structural highlights

2h5g is a 2 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 2.25Å
Ligands:	MSE, SO4
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

P5CS_HUMAN Defects in ALDH18A1 are the cause of cutis laxa, autosomal recessive, type 3A (ARCL3A) [MIM:219150. A syndrome characterized by facial dysmorphism with a progeroid appearance, large and late-closing fontanel, cutis laxa, joint hyperlaxity, athetoid movements and hyperreflexia, pre- and postnatal growth retardation, intellectual deficit, developmental delay, and ophthalmologic abnormalities.^[1] ^[2]

Function

P5CS_HUMAN Bifunctional enzyme that converts glutamate to glutamate 5-semialdehyde, an intermediate in the biosynthesis of proline, ornithine and arginine.^[3] ^[4]

Evolutionary Conservation

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

References

↑ Baumgartner MR, Hu CA, Almashanu S, Steel G, Obie C, Aral B, Rabier D, Kamoun P, Saudubray JM, Valle D. Hyperammonemia with reduced ornithine, citrulline, arginine and proline: a new inborn error caused by a mutation in the gene encoding delta(1)-pyrroline-5-carboxylate synthase. Hum Mol Genet. 2000 Nov 22;9(19):2853-8. PMID:11092761
↑ Bicknell LS, Pitt J, Aftimos S, Ramadas R, Maw MA, Robertson SP. A missense mutation in ALDH18A1, encoding Delta1-pyrroline-5-carboxylate synthase (P5CS), causes an autosomal recessive neurocutaneous syndrome. Eur J Hum Genet. 2008 Oct;16(10):1176-86. doi: 10.1038/ejhg.2008.91. Epub 2008, May 14. PMID:18478038 doi:10.1038/ejhg.2008.91
↑ Hu CA, Lin WW, Obie C, Valle D. Molecular enzymology of mammalian Delta1-pyrroline-5-carboxylate synthase. Alternative splice donor utilization generates isoforms with different sensitivity to ornithine inhibition. J Biol Chem. 1999 Mar 5;274(10):6754-62. PMID:10037775
↑ Baumgartner MR, Hu CA, Almashanu S, Steel G, Obie C, Aral B, Rabier D, Kamoun P, Saudubray JM, Valle D. Hyperammonemia with reduced ornithine, citrulline, arginine and proline: a new inborn error caused by a mutation in the gene encoding delta(1)-pyrroline-5-carboxylate synthase. Hum Mol Genet. 2000 Nov 22;9(19):2853-8. PMID:11092761

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OCA

[1] Baumgartner MR, Hu CA, Almashanu S, Steel G, Obie C, Aral B, Rabier D, Kamoun P, Saudubray JM, Valle D. Hyperammonemia with reduced ornithine, citrulline, arginine and proline: a new inborn error caused by a mutation in the gene encoding delta(1)-pyrroline-5-carboxylate synthase. Hum Mol Genet. 2000 Nov 22;9(19):2853-8. PMID:11092761

[2] Bicknell LS, Pitt J, Aftimos S, Ramadas R, Maw MA, Robertson SP. A missense mutation in ALDH18A1, encoding Delta1-pyrroline-5-carboxylate synthase (P5CS), causes an autosomal recessive neurocutaneous syndrome. Eur J Hum Genet. 2008 Oct;16(10):1176-86. doi: 10.1038/ejhg.2008.91. Epub 2008, May 14. PMID:18478038 doi:10.1038/ejhg.2008.91

[3] Hu CA, Lin WW, Obie C, Valle D. Molecular enzymology of mammalian Delta1-pyrroline-5-carboxylate synthase. Alternative splice donor utilization generates isoforms with different sensitivity to ornithine inhibition. J Biol Chem. 1999 Mar 5;274(10):6754-62. PMID:10037775

[4] Baumgartner MR, Hu CA, Almashanu S, Steel G, Obie C, Aral B, Rabier D, Kamoun P, Saudubray JM, Valle D. Hyperammonemia with reduced ornithine, citrulline, arginine and proline: a new inborn error caused by a mutation in the gene encoding delta(1)-pyrroline-5-carboxylate synthase. Hum Mol Genet. 2000 Nov 22;9(19):2853-8. PMID:11092761

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[2]

[3]

[4]

@@ Line 1: / Line 1: @@
-[[Image:2h5g.gif|left|200px]]<br />
-<applet load="2h5g" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="2h5g, resolution 2.25&Aring;" />
-'''Crystal structure of human pyrroline-5-carboxylate synthetase'''<br />
-==Disease==
+==Crystal structure of human pyrroline-5-carboxylate synthetase==
-Known diseases associated with this structure: Hyperammonemia with hypoornithinemia, hypocitrullinemia, hypoargininemia, and hypoprolinemia OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=138250 138250]]
+<StructureSection load='2h5g' size='340' side='right'caption='[[2h5g]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
+== Structural highlights ==
-==About this Structure==
+<table><tr><td colspan='2'>[[2h5g]] is a 2 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=2H5G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H5G FirstGlance]. <br>
-H5G is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glutamate-5-semialdehyde_dehydrogenase Glutamate-5-semialdehyde dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.41 1.2.1.41] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2H5G OCA].
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25&#8491;</td></tr>
-[[Category: Glutamate-5-semialdehyde dehydrogenase]]
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=2h5g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h5g OCA], [https://pdbe.org/2h5g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h5g RCSB], [https://www.ebi.ac.uk/pdbsum/2h5g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h5g ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[https://www.uniprot.org/uniprot/P5CS_HUMAN P5CS_HUMAN] Defects in ALDH18A1 are the cause of cutis laxa, autosomal recessive, type 3A (ARCL3A) [MIM:[https://omim.org/entry/219150 219150]. A syndrome characterized by facial dysmorphism with a progeroid appearance, large and late-closing fontanel, cutis laxa, joint hyperlaxity, athetoid movements and hyperreflexia, pre- and postnatal growth retardation, intellectual deficit, developmental delay, and ophthalmologic abnormalities.<ref>PMID:11092761</ref> <ref>PMID:18478038</ref>
+== Function ==
+[https://www.uniprot.org/uniprot/P5CS_HUMAN P5CS_HUMAN] Bifunctional enzyme that converts glutamate to glutamate 5-semialdehyde, an intermediate in the biosynthesis of proline, ornithine and arginine.<ref>PMID:10037775</ref> <ref>PMID:11092761</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/h5/2h5g_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2h5g ConSurf].
+<div style="clear:both"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Arrowsmith, C.]]
+[[Category: Arrowsmith C]]
-[[Category: Berridge, G.]]
+[[Category: Berridge G]]
-[[Category: Bray, J.]]
+[[Category: Bray J]]
-[[Category: Edwards, A.]]
+[[Category: Edwards A]]
-[[Category: Gileadi, O.]]
+[[Category: Gileadi O]]
-[[Category: Gorrec, F.]]
+[[Category: Gorrec F]]
-[[Category: Hozjan, V.]]
+[[Category: Hozjan V]]
-[[Category: Kavanagh, K.]]
+[[Category: Kavanagh K]]
-[[Category: Oppermann, U.]]
+[[Category: Oppermann U]]
-[[Category: Papagrigoriou, E.]]
+[[Category: Papagrigoriou E]]
-[[Category: SGC, Structural.Genomics.Consortium.]]
+[[Category: Shafqat N]]
-[[Category: Shafqat, N.]]
+[[Category: Smee C]]
-[[Category: Smee, C.]]
+[[Category: Sundstrom M]]
-[[Category: Sundstrom, M.]]
+[[Category: Turnbull AP]]
-[[Category: Turnbull, A.P.]]
+[[Category: Weigelt J]]
-[[Category: Weigelt, J.]]
-[[Category: SO4]]
-[[Category: dehydrogenase]]
-[[Category: sgc]]
-[[Category: structural genomics]]
-[[Category: structural genomics consortium]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:26:56 2007''

2h5g: Difference between revisions

Latest revision as of 08:06, 30 October 2024

Crystal structure of human pyrroline-5-carboxylate synthetase

Structural highlights

Disease

Function

Evolutionary Conservation

References

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