From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1fp3.jpg|left|200px]] | + | {{Seed}} |
| | + | [[Image:1fp3.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1fp3| PDB=1fp3 | SCENE= }} | | {{STRUCTURE_1fp3| PDB=1fp3 | SCENE= }} |
| | | | |
| - | '''CRYSTAL STRUCTURE OF N-ACYL-D-GLUCOSAMINE 2-EPIMERASE FROM PORCINE KIDNEY'''
| + | ===CRYSTAL STRUCTURE OF N-ACYL-D-GLUCOSAMINE 2-EPIMERASE FROM PORCINE KIDNEY=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | The X-ray crystallographic structure of N-acyl-d-glucosamine 2-epimerase (AGE) from porcine kidney, which has been identified to be a renin-binding protein (RnBP), was determined by the multiple isomorphous replacement method and refined at 2.0 A resolution with a final R-factor of 16.9 % for 15 to 2.0 A resolution data. The refined structure of AGE comprised 804 amino acid residues (one dimer) and 145 water molecules. The dimer of AGE had an asymmetric unit with approximate dimensions 46 Ax48 Ax96 A. The AGE monomer is composed of an alpha(6)/alpha(6)-barrel, the structure of which is found in glucoamylase and cellulase. One side of the AGE alpha(6)/alpha(6)-barrel structure comprises long loops containing five short beta-sheets, and contributes to the formation of a deep cleft shaped like a funnel. The putative active-site pocket and a possible binding site for the substrate N-acetyl-d-glucosamine (GlcNAc) were found in the cleft. The other side of the alpha(6)/alpha(6)-barrel comprises short loops and contributes to the dimer formation. At the dimer interface, which is composed of the short loops and alpha-helices of the subunits, five strong ion-pair interactions were observed, which play a major role in the dimer assembly. This completely ruled out the previously accepted hypothesis that the formation of the RnBP homodimer and RnBP-renin heterodimer requires the leucine zipper motif present in RnBP. | + | The line below this paragraph, {{ABSTRACT_PUBMED_11061972}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11061972 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_11061972}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 31: |
Line 35: |
| | [[Category: Alpha/alpha-barrel]] | | [[Category: Alpha/alpha-barrel]] |
| | [[Category: N-acyl-d-glucosamine 2-epimerase]] | | [[Category: N-acyl-d-glucosamine 2-epimerase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:35:52 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:43:01 2008'' |
Revision as of 00:43, 1 July 2008
Template:STRUCTURE 1fp3
CRYSTAL STRUCTURE OF N-ACYL-D-GLUCOSAMINE 2-EPIMERASE FROM PORCINE KIDNEY
Template:ABSTRACT PUBMED 11061972
About this Structure
1FP3 is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.
Reference
Crystal structure of N-acyl-D-glucosamine 2-epimerase from porcine kidney at 2.0 A resolution., Itoh T, Mikami B, Maru I, Ohta Y, Hashimoto W, Murata K, J Mol Biol. 2000 Nov 10;303(5):733-44. PMID:11061972
Page seeded by OCA on Tue Jul 1 03:43:01 2008
