This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

1b1u

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 15:03, 2 June 2021

CRYSTAL STRUCTURE OF THE BIFUNCTIONAL INHIBITOR RAGI

Structural highlights

1b1u is a 1 chain structure with sequence from Eleusine coracana. This structure supersedes the now removed PDB entry 1jfo. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1b1u"

@@ Line 3: / Line 3: @@
 <StructureSection load='1b1u' size='340' side='right'caption='[[1b1u]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == 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='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>
 == 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 ==
 [[Image:Consurf_key_small.gif|200px|right]]

1b1u

From Proteopedia

Revision as of 15:03, 2 June 2021

CRYSTAL STRUCTURE OF THE BIFUNCTIONAL INHIBITOR RAGI

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox