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.


1m8g

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1m8g.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1m8g.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1m8g| PDB=1m8g | SCENE= }}
{{STRUCTURE_1m8g| PDB=1m8g | SCENE= }}
-
'''Crystal Structure Of Methanobacterium Thermoautotrophicum Nicotinamide Mononucleotide Adenylyltransferase Mutant R11K complexed with NAD'''
+
===Crystal Structure Of Methanobacterium Thermoautotrophicum Nicotinamide Mononucleotide Adenylyltransferase Mutant R11K complexed with NAD===
-
==Overview==
+
<!--
-
Several residues lining the ATP-binding site of Methanobacterium thermoautotrophicum nicotinamide mononucleotide adenylyltransferase (NMNATase) were mutated in an effort to better characterize their roles in substrate binding and catalysis. Residues selected were Arg-11 and Arg-136, both of which had previously been implicated as substrate binding residues, as well as His-16 and His-19, part of the HXGH active site motif and postulated to be of importance in catalysis. Kinetic studies revealed that both Arg-11 and Arg-136 contributed to the binding of the substrate, ATP. When these amino acids were replaced by lysines, the apparent Km values of the respective mutants for ATP decreased by factors of 1.3 and 2.9 and by factors of 1.9 and 8.8 when the same residues were changed to alanines. All four Arg mutants displayed unaltered Km values for NMN. The apparent kcat values of the R11K and R136K mutants were the same as those of WT NMNATase but the apparent kcat values of the alanine mutants had decreased. Crystal structures of the Arg mutants revealed NAD+ and SO42- molecules trapped at their active sites. The binding interactions of NAD+ were unchanged but the binding of SO42- was altered in these mutants compared with wild type. The alanine mutants at positions His-16 and His-19 retained approximately 6 and 1.3%, respectively, of WT NMNATase activity indicating that His-19 is a key catalytic group. Surprisingly, this H19A mutant displayed a novel and distinct mode of NAD+ binding when co-crystallized in the presence of NAD+ and SO42-.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12810729}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12810729 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12810729}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Hxgh motif]]
[[Category: Hxgh motif]]
[[Category: Nucleotidyltransferase]]
[[Category: Nucleotidyltransferase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:45:39 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 23:26:02 2008''

Revision as of 20:26, 2 July 2008

Image:1m8g.png

Template:STRUCTURE 1m8g

Crystal Structure Of Methanobacterium Thermoautotrophicum Nicotinamide Mononucleotide Adenylyltransferase Mutant R11K complexed with NAD

Template:ABSTRACT PUBMED 12810729

About this Structure

1M8G is a Single protein structure of sequence from Methanothermobacter thermautotrophicus. Full crystallographic information is available from OCA.

Reference

Mutational, structural, and kinetic studies of the ATP-binding site of Methanobacterium thermoautotrophicum nicotinamide mononucleotide adenylyltransferase., Saridakis V, Pai EF, J Biol Chem. 2003 Sep 5;278(36):34356-63. Epub 2003 Jun 16. PMID:12810729

Page seeded by OCA on Wed Jul 2 23:26:02 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1m8g"
Personal tools