1byd: Difference between revisions

Revision as of 19:54, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1byd.png

Template:STRUCTURE 1byd

CRYSTAL STRUCTURES OF SOYBEAN BETA-AMYLASE REACTED WITH BETA-MALTOSE AND MALTAL: ACTIVE SITE COMPONENTS AND THEIR APPARENT ROLE IN CATALYSISCRYSTAL STRUCTURES OF SOYBEAN BETA-AMYLASE REACTED WITH BETA-MALTOSE AND MALTAL: ACTIVE SITE COMPONENTS AND THEIR APPARENT ROLE IN CATALYSIS

Template:ABSTRACT PUBMED 8011643

About this StructureAbout this Structure

1BYD is a Single protein structure of sequence from Glycine max. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structures of soybean beta-amylase reacted with beta-maltose and maltal: active site components and their apparent roles in catalysis., Mikami B, Degano M, Hehre EJ, Sacchettini JC, Biochemistry. 1994 Jun 28;33(25):7779-87. PMID:8011643

Page seeded by OCA on Mon Jun 30 19:54:55 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1byd.jpg|left|200px]]
+{{Seed}}
+[[Image:1byd.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1byd|  PDB=1byd  |  SCENE=  }}
-'''CRYSTAL STRUCTURES OF SOYBEAN BETA-AMYLASE REACTED WITH BETA-MALTOSE AND MALTAL: ACTIVE SITE COMPONENTS AND THEIR APPARENT ROLE IN CATALYSIS'''
+===CRYSTAL STRUCTURES OF SOYBEAN BETA-AMYLASE REACTED WITH BETA-MALTOSE AND MALTAL: ACTIVE SITE COMPONENTS AND THEIR APPARENT ROLE IN CATALYSIS===
-==Overview==
+<!--
-The crystal structures of catalytically competent soybean beta-amylase, unliganded and bathed with small substrates (beta-maltose, maltal), were determined at 1.9-2.2-A resolution. Two molecules of beta-maltose substrate bind to the protein in tandem, with some maltotetraose enzymic condensation product sharing the same binding sites. The beta-amylase soaked with maltal shows a similar arrangement of two bound molecules of 2-deoxymaltose, the enzymic hydration product. In each case the nonreducing ends of the saccharide ligands are oriented toward the base of the protein's active site pocket. The catalytic center, located between the bound disaccharides and found deeper in the pocket than where the inhibitor alpha-cyclodextrin binds, is characterized by the presence of oppositely disposed carboxyl groups of two conserved glutamic acid residues. The OE2 carboxyl of Glu 186 is below the plane of the penultimate glucose residue (Glc 2) of bound maltotetraose, 2.6 A from the oxygen atom of that ligand's penultimate alpha-1,4-glucosidic linkage. The OE2 carboxyl of Glu 380 lies above the plane of Glc 2, 2.8 A from the O-1 atom of the more deeply bound beta-maltose. Saccharide binding does not alter the spatial coordinates of these two carboxyl groups or the overall conformation of the 57-kDa protein. However, the saccharide complexes of the active enzyme are associated with a significant (10 A) local conformational change in a peptide segment of a loop (L3) that borders the active site pocket.(ABSTRACT TRUNCATED AT 250 WORDS)
+The line below this paragraph, {{ABSTRACT_PUBMED_8011643}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 8011643 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_8011643}}
 ==About this Structure==
@@ Line 27: / Line 31: @@
 [[Category: Mikami, B.]]
 [[Category: Sacchettini, J C.]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 12:06:54 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:54:55 2008''