English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
 
 
DownloadE-Mail
 Local TagsRelease HistoryDetailsSummary
  Structures of active conformations of UMP kinase from Dictyostelium discoideum suggest phosphoryl transfer is associative

Schlichting, I., & Reinstein, J. (1997). Structures of active conformations of UMP kinase from Dictyostelium discoideum suggest phosphoryl transfer is associative. Biochemistry, 36(31), 9290-9296. doi:10.1021/bi970974c.

Item is

 

show all hide all

Basic

show hide
Item Permalink: https://hdl.handle.net/11858/00-001M-0000-002C-2351-3 Version Permalink: https://hdl.handle.net/11858/00-001M-0000-002C-2352-1
Genre: Journal Article

Files

show Files
hide Files
:
Biochem_36_1997_9290.pdf (Any fulltext), 334KB
 
File Permalink:
-
Name:
Biochem_36_1997_9290.pdf
Description:
-
OA-Status:
Visibility:
Restricted (Max Planck Institute for Medical Research, MHMF; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show
hide
Locator:
http://pubs.acs.org/doi/pdf/10.1021/bi970974c (Any fulltext)
Description:
-
OA-Status:
Locator:
https://dx.doi.org/10.1021/bi970974c (Any fulltext)
Description:
-
OA-Status:

Creators

show
hide
 Creators:
Schlichting, Ilme1, Author           
Reinstein, Jochen2, Author           
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              
2Molecular chaperones, Max Planck Institute for Medical Research, Max Planck Society, ou_1497728              

Content

show
hide
Free keywords: -
 Abstract: UMP/CMP kinase from Dictyostelium discoideum (UmpKdicty) catalyzes the specific transfer of the terminal phosphate of ATP to UMP or CMP. Crystal structures of UmpKdicty with substrates and the transition state analogs AlF3 or BeF2 that lock UmpKdicty in active conformations were solved. The positions of the catalytic Mg2+ and the highly conserved lysine of the P loop are virtually invariant in the different structures. In contrast, catalytic arginines move to stabilize charges that develop during this reaction. The location of the arginines indicates formation of negative charges during the reaction at the transferred phosphoryl group, but not at the phosphate bridging oxygen atoms. This is consistent with an associative phosphoryl transfer mechanism but not with a dissociative one.

Details

show
hide
Language(s): eng - English
 Dates: 1997-06-091997-04-251997-08-05
 Publication Status: Issued
 Pages: 7
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1021/bi970974c
URI: https://www.ncbi.nlm.nih.gov/pubmed/9280438
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Biochemistry
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Columbus, Ohio : American Chemical Society
Pages: - Volume / Issue: 36 (31) Sequence Number: - Start / End Page: 9290 - 9296 Identifier: ISSN: 0006-2960
CoNE: https://pure.mpg.de/cone/journals/resource/954925384103