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| | ==Crystal structure of pea prolegumin, an 11S seed globulin from Pisum sativum L.== | | ==Crystal structure of pea prolegumin, an 11S seed globulin from Pisum sativum L.== |
| - | <StructureSection load='3ksc' size='340' side='right' caption='[[3ksc]], [[Resolution|resolution]] 2.61Å' scene=''> | + | <StructureSection load='3ksc' size='340' side='right'caption='[[3ksc]], [[Resolution|resolution]] 2.61Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3ksc]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Garden_pea Garden pea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KSC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3KSC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3ksc]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KSC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KSC FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.606Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">legA, Plant gene ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3888 Garden pea])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ksc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ksc OCA], [http://pdbe.org/3ksc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ksc RCSB], [http://www.ebi.ac.uk/pdbsum/3ksc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ksc ProSAT]</span></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=3ksc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ksc OCA], [https://pdbe.org/3ksc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ksc RCSB], [https://www.ebi.ac.uk/pdbsum/3ksc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ksc ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/LEGA_PEA LEGA_PEA] This protein found in the seeds of many leguminous and non-leguminous plants is the source of sulfur-containing amino acids in seed meals. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Garden pea]] | + | [[Category: Large Structures]] |
| - | [[Category: Cabanos, C]] | + | [[Category: Pisum sativum]] |
| - | [[Category: Fukuda, C]] | + | [[Category: Cabanos C]] |
| - | [[Category: Fukuda, T]] | + | [[Category: Fukuda C]] |
| - | [[Category: Itoh, T]] | + | [[Category: Fukuda T]] |
| - | [[Category: Kimura, A]] | + | [[Category: Itoh T]] |
| - | [[Category: Maruyama, N]] | + | [[Category: Kimura A]] |
| - | [[Category: Mikami, B]] | + | [[Category: Maruyama N]] |
| - | [[Category: Prak, K]] | + | [[Category: Mikami B]] |
| - | [[Category: Tandang-Silvas, M R.G]] | + | [[Category: Prak K]] |
| - | [[Category: Utsumi, S]] | + | [[Category: Tandang-Silvas MRG]] |
| - | [[Category: 11s seed storage protein]]
| + | [[Category: Utsumi S]] |
| - | [[Category: Pea prolegumin]]
| + | |
| - | [[Category: Pisum sativum l]]
| + | |
| - | [[Category: Plant protein]]
| + | |
| - | [[Category: Seed storage protein]]
| + | |
| - | [[Category: Storage protein]]
| + | |
| Structural highlights
Function
LEGA_PEA This protein found in the seeds of many leguminous and non-leguminous plants is the source of sulfur-containing amino acids in seed meals.
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 crystal structures of two pro-11S globulins namely: rapeseed procruciferin and pea prolegumin are presented here. We have extensively compared them with the other known structures of plant seed 11S and 7S globulins. In general, the disordered regions in the crystal structures among the 11S globulins correspond to their five variable regions. Variable region III of procruciferin is relatively short and is in a loop conformation. This region is highly disordered in other pro-11S globulin crystals. Local helical and strand variations also occur across the group despite general structure conservation. We showed how these variations may alter specific physicochemical, functional and physiological properties. Aliphatic hydrophobic residues on the molecular surface correlate well with Tm values of the globulins. We also considered other structural features that were reported to influence thermal stability but no definite conclusion was drawn since each factor has additive or subtractive effect. Comparison between proA3B4 and mature A3B4 revealed an increase in r.m.s.d. values near variable regions II and IV. Both regions are on the IE face. Secondary structure based alignment of 11S and 7S globulins revealed 16 identical residues. Based on proA3B4 sequence, Pro60, Gly128, Phe163, Phe208, Leu213, Leu227, Ile237, Pro382, Val404, Pro425 and Val 466 are involved in trimer formation and stabilization. Gly28, Gly74, Asp135, Gly349 and Gly397 are involved in correct globular folding.
Conservation and divergence on plant seed 11S globulins based on crystal structures.,Tandang-Silvas MR, Fukuda T, Fukuda C, Prak K, Cabanos C, Kimura A, Itoh T, Mikami B, Utsumi S, Maruyama N Biochim Biophys Acta. 2010 Jul;1804(7):1432-42. Epub 2010 Mar 6. PMID:20215054[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tandang-Silvas MR, Fukuda T, Fukuda C, Prak K, Cabanos C, Kimura A, Itoh T, Mikami B, Utsumi S, Maruyama N. Conservation and divergence on plant seed 11S globulins based on crystal structures. Biochim Biophys Acta. 2010 Jul;1804(7):1432-42. Epub 2010 Mar 6. PMID:20215054 doi:10.1016/j.bbapap.2010.02.016
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