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.


1j9w

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1j9w.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1j9w.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1j9w| PDB=1j9w | SCENE= }}
{{STRUCTURE_1j9w| PDB=1j9w | SCENE= }}
-
'''Solution Structure of the CAI Michigan 1 Variant'''
+
===Solution Structure of the CAI Michigan 1 Variant===
-
==Overview==
+
<!--
-
The human genetic variant carbonic anhydrase I (CA I) Michigan 1 results from a single point mutation that changes His 67 to Arg in a critical region of the active site. This variant of the zinc metalloenzyme appears to be unique in that it possesses an esterase activity that is specifically enhanced by added free zinc ions. We have determined the three-dimensional structure of human CA I Michigan 1 by X-ray crystallography to a resolution of 2.6 A. In the absence of added zinc ions, the mutated residue, Arg 67, points out of the active site, hydrogen bonding with the carboxylate of Asn 69. This contrasts with the orientation of His 67, in the native isozyme, which points into the active site. The orientations of His 94, His 96, and His 119, that coordinate the catalytic zinc ion, and of the catalytically critical Thr 199-Glu 106 hydrogen bonding system, are largely unchanged in the mutant. The structure of an enzyme adduct with a second zinc bound was determined to a resolution of 2.0 A. The second zinc ion is coordinated to His 64, His 200, and Arg 67. This arginine residue reverses its orientation on zinc binding and turns into the active site. The residues at these three positions have been implicated in determining the specific kinetic properties of native CA I. This is, to our knowledge, the first example of a zinc ion coordinating with an arginine residue in a Zn(II) enzyme.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12009884}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12009884 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12009884}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Tilli, S.]]
[[Category: Tilli, S.]]
[[Category: 10-stranded-beta-sheet]]
[[Category: 10-stranded-beta-sheet]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:57:40 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 14:46:23 2008''

Revision as of 11:46, 1 July 2008

Image:1j9w.png

Template:STRUCTURE 1j9w

Solution Structure of the CAI Michigan 1 Variant

Template:ABSTRACT PUBMED 12009884

About this Structure

1J9W is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of a zinc-activated variant of human carbonic anhydrase I, CA I Michigan 1: evidence for a second zinc binding site involving arginine coordination., Ferraroni M, Tilli S, Briganti F, Chegwidden WR, Supuran CT, Wiebauer KE, Tashian RE, Scozzafava A, Biochemistry. 2002 May 21;41(20):6237-44. PMID:12009884

Page seeded by OCA on Tue Jul 1 14:46:23 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1j9w"
Personal tools