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| | <StructureSection load='1b1u' size='340' side='right'caption='[[1b1u]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='1b1u' size='340' side='right'caption='[[1b1u]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1b1u]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Eleusine_coracana Eleusine coracana]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1jfo 1jfo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B1U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1B1U FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1b1u]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Eleusine_coracana Eleusine coracana]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1jfo 1jfo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B1U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B1U FirstGlance]. <br> |
| - | </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=1b1u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b1u OCA], [http://pdbe.org/1b1u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1b1u RCSB], [http://www.ebi.ac.uk/pdbsum/1b1u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1b1u ProSAT]</span></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]] 2.2Å</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=1b1u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b1u OCA], [https://pdbe.org/1b1u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b1u RCSB], [https://www.ebi.ac.uk/pdbsum/1b1u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b1u ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/IAAT_ELECO IAAT_ELECO]] May play a protective role against endo- and exogenous hydrolytic activities in the Ragi seeds. | + | [https://www.uniprot.org/uniprot/IAAT_ELECO IAAT_ELECO] May play a protective role against endo- and exogenous hydrolytic activities in the Ragi seeds. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | [[Category: Eleusine coracana]] | | [[Category: Eleusine coracana]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Gourinath, S]] | + | [[Category: Gourinath S]] |
| - | [[Category: Singh, T P]] | + | [[Category: Singh TP]] |
| - | [[Category: Srinivasan, A]] | + | [[Category: Srinivasan A]] |
| - | [[Category: Bifunctional]]
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| - | [[Category: Hydrolase inhibitor]]
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| Structural highlights
Function
IAAT_ELECO May play a protective role against endo- and exogenous hydrolytic activities in the Ragi seeds.
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 structure of a bifunctional inhibitor of alpha-amylase and trypsin (RATI) from ragi seeds (Indian finger millet, Eleusine coracana Gaertneri) has been determined by X-ray diffraction at 2.2 A resolution. The inhibitor consists of 122 amino acids, with five disulfide bridges, and belongs to the plant alpha-amylase/trypsin inhibitor family. The crystals were grown by the microdialysis method using ammonium sulfate as a precipitating agent. The structure was determined by the molecular-replacement method using as models the structures of Corn Hageman factor inhibitor (CHFI) and of RATI at 2.9 A resolution determined previously. It has been refined to an R factor of 21.9%. The structure shows an r.m.s. deviation for C(alpha) atoms of 2.0 A compared with its own NMR structure, whereas the corresponding value compared with CHFI is found to be 1.4 A. The r.m.s. difference for C(alpha) atoms when compared with the same protein in the structure of the complex with alpha-amylase is 0.7 A. The conformations of trypsin-binding loop and the alpha-amylase-binding N-terminal region were also found to be similar in the crystal structures of native RATI and its complex with alpha-amylase. These regions differed considerably in the NMR structure.
Structure of the bifunctional inhibitor of trypsin and alpha-amylase from ragi seeds at 2.2 A resolution.,Gourinath S, Alam N, Srinivasan A, Betzel C, Singh TP Acta Crystallogr D Biol Crystallogr. 2000 Mar;56(Pt 3):287-93. PMID:10713515[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Gourinath S, Alam N, Srinivasan A, Betzel C, Singh TP. Structure of the bifunctional inhibitor of trypsin and alpha-amylase from ragi seeds at 2.2 A resolution. Acta Crystallogr D Biol Crystallogr. 2000 Mar;56(Pt 3):287-93. PMID:10713515
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