1ckn: Difference between revisions

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~~'''~~STRUCTURE OF GUANYLYLATED MRNA CAPPING ENZYME COMPLEXED WITH GTP~~'''~~

===STRUCTURE OF GUANYLYLATED MRNA CAPPING ENZYME COMPLEXED WITH GTP===

~~==Overview==~~

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~~We have solved the crystal structure of an mRNA capping enzyme at 2.5 A resolution.~~ The ~~enzyme comprises two domains with a deep~~, ~~but narrow~~, ~~cleft between them. The two molecules in~~ the ~~crystallographic asymmetric unit adopt very different conformations; both contain a bound GTP, but one protein molecule is in an open conformation while~~ the ~~other is in a closed conformation~~. ~~Only in the closed conformation~~ is the enzyme able to bind manganese ions and undergo catalysis within the crystals to yield the covalent guanylated enzyme intermediate. These structures provide direct evidence for a mechanism that involves a significant conformational change in the enzyme during catalysis.

The line below this paragraph, {{ABSTRACT_PUBMED_9160746}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 9160746 is the PubMed ID number.

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==About this Structure==

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[[Category: Mrna]]

[[Category: Nucleotidyltransferase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 12~~:50:10 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:52:32 2008''

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-[[Image:1ckn.gif|left|200px]]
+{{Seed}}
+[[Image:1ckn.png|left|200px]]
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 {{STRUCTURE_1ckn|  PDB=1ckn  |  SCENE=  }}
-'''STRUCTURE OF GUANYLYLATED MRNA CAPPING ENZYME COMPLEXED WITH GTP'''
+===STRUCTURE OF GUANYLYLATED MRNA CAPPING ENZYME COMPLEXED WITH GTP===
-==Overview==
+<!--
-We have solved the crystal structure of an mRNA capping enzyme at 2.5 A resolution. The enzyme comprises two domains with a deep, but narrow, cleft between them. The two molecules in the crystallographic asymmetric unit adopt very different conformations; both contain a bound GTP, but one protein molecule is in an open conformation while the other is in a closed conformation. Only in the closed conformation is the enzyme able to bind manganese ions and undergo catalysis within the crystals to yield the covalent guanylated enzyme intermediate. These structures provide direct evidence for a mechanism that involves a significant conformational change in the enzyme during catalysis.
+The line below this paragraph, {{ABSTRACT_PUBMED_9160746}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9160746 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9160746}}
 ==About this Structure==
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 [[Category: Mrna]]
 [[Category: Nucleotidyltransferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 12:50:10 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:52:32 2008''