From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1kop.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1kop.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1kop| PDB=1kop | SCENE= }} | | {{STRUCTURE_1kop| PDB=1kop | SCENE= }} |
| | | | |
| - | '''NEISSERIA GONORRHOEAE CARBONIC ANHYDRASE'''
| + | ===NEISSERIA GONORRHOEAE CARBONIC ANHYDRASE=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | The crystal structure of carbonic anhydrase from Neisseria gonorrhoeae has been solved to a resolution of 1.78 A by molecular replacement using human carbonic anhydrase II as a template. After refinement the R factor was 17.8% (Rfree=23.2%). There are two molecules per asymmetric unit (space group P21), but they have essentially identical structures. The fold of the N. gonorrhoeae enzyme is very similar to that of human isozyme II; 192 residues, 74 of which are identical in the two enzymes, have equivalent positions in the three-dimensional structures. This corresponds to 85% of the entire polypeptide chain of the bacterial enzyme. The only two cysteine residues in the bacterial enzyme, which has a periplasmic location in the cell, are connected by a disulfide bond. Most of the secondary structure elements present in human isozyme II are retained in N. gonorrhoeae carbonic anhydrase, but there are also differences, particularly in the few helical regions. Long deletions in the bacterial enzyme relative to human isozyme II have resulted in a considerable shortening of three surface loops. One of these deletions, corresponding to residues 128 to 139 in the human enzyme, leads to a widening of the entrance to the hydrophobic part of the active site cavity. Practically all the amino acid residues in the active site of human isozyme II are conserved in the N. gonorrhoeae enzyme and have similar structural positions. However, the imidazole ring of a histidine residue, which has been shown to function as a proton shuttle in the catalytic mechanism of the human enzyme, interacts with an extraneous entity, which has tentatively been identified as a 2-mercaptoethanol molecule from the crystallization medium. When this entity is removed by soaking the crystal in a different medium, the side-chain of His66 becomes quite mobile. The structure of a complex with the sulfonamide inhibitor, acetazolamide, has also been determined. Its position in the active site is very similar to that observed in human carbonic anhydrase II. | + | The line below this paragraph, {{ABSTRACT_PUBMED_9761692}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 9761692 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_9761692}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 32: |
Line 36: |
| | [[Category: Neisseria gonorrhoeae]] | | [[Category: Neisseria gonorrhoeae]] |
| | [[Category: Structural trimming]] | | [[Category: Structural trimming]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:59:28 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:40:11 2008'' |
Revision as of 07:40, 2 July 2008
Template:STRUCTURE 1kop
NEISSERIA GONORRHOEAE CARBONIC ANHYDRASE
Template:ABSTRACT PUBMED 9761692
About this Structure
1KOP is a Single protein structure of sequence from Neisseria gonorrhoeae. Full crystallographic information is available from OCA.
Reference
Crystal structure of carbonic anhydrase from Neisseria gonorrhoeae and its complex with the inhibitor acetazolamide., Huang S, Xue Y, Sauer-Eriksson E, Chirica L, Lindskog S, Jonsson BH, J Mol Biol. 1998;283(1):301-10. PMID:9761692
Page seeded by OCA on Wed Jul 2 10:40:11 2008
