2v8i: Difference between revisions

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[[Image:2v8i.~~jpg~~|left|200px]]

[[Image:2v8i.png|left|200px]]

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~~'''~~STRUCTURE OF A FAMILY 2 PECTATE LYASE IN A NATIVE FORM~~'''~~

===STRUCTURE OF A FAMILY 2 PECTATE LYASE IN A NATIVE FORM===

~~==Overview==~~

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The ~~family 2 pectate lyase from Yersinia enterocolitica (YePL2A)~~, ~~solved to 1.5A~~, ~~reveals it to be~~ the ~~first prokaryotic protein reported~~ to ~~display~~ the ~~rare~~ (~~alpha~~/~~alpha)(7) barrel fold~~. ~~In addition to its apo form, we have also determined the structure of a metal-bound form of YePL2A (to 2~~.0A) and a trigalacturonic acid-bound substrate complex (to 2.1A) Although its fold is rare, the catalytic center of YePL2A can be superimposed with structurally unrelated families, underlining the conserved catalytic amino acid architecture of the beta-elimination mechanism. In addition to its overall structure, YePL2A also has two other unique features: 1) it utilizes a metal atom other than calcium for catalysis, ~~and 2) its Bronstead base~~ is ~~in an alternate conformation and directly interacts with~~ the ~~uronate group of the substrate~~.

The line below this paragraph, {{ABSTRACT_PUBMED_17881361}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 17881361 is the PubMed ID number.

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==About this Structure==

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[[Category: Pectin degradation]]

[[Category: Periplasm]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun ~~May 4 18~~:22:24 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 16:29:24 2008''

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-[[Image:2v8i.jpg|left|200px]]
+{{Seed}}
+[[Image:2v8i.png|left|200px]]
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 {{STRUCTURE_2v8i|  PDB=2v8i  |  SCENE=  }}
-'''STRUCTURE OF A FAMILY 2 PECTATE LYASE IN A NATIVE FORM'''
+===STRUCTURE OF A FAMILY 2 PECTATE LYASE IN A NATIVE FORM===
-==Overview==
+<!--
-The family 2 pectate lyase from Yersinia enterocolitica (YePL2A), solved to 1.5A, reveals it to be the first prokaryotic protein reported to display the rare (alpha/alpha)(7) barrel fold. In addition to its apo form, we have also determined the structure of a metal-bound form of YePL2A (to 2.0A) and a trigalacturonic acid-bound substrate complex (to 2.1A) Although its fold is rare, the catalytic center of YePL2A can be superimposed with structurally unrelated families, underlining the conserved catalytic amino acid architecture of the beta-elimination mechanism. In addition to its overall structure, YePL2A also has two other unique features: 1) it utilizes a metal atom other than calcium for catalysis, and 2) its Bronstead base is in an alternate conformation and directly interacts with the uronate group of the substrate.
+The line below this paragraph, {{ABSTRACT_PUBMED_17881361}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17881361 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17881361}}
 ==About this Structure==
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 [[Category: Pectin degradation]]
 [[Category: Periplasm]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 18:22:24 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 16:29:24 2008''