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.


1nnl

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1nnl.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1nnl.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1nnl| PDB=1nnl | SCENE= }}
{{STRUCTURE_1nnl| PDB=1nnl | SCENE= }}
-
'''Crystal structure of Human Phosphoserine Phosphatase'''
+
===Crystal structure of Human Phosphoserine Phosphatase===
-
==Overview==
+
<!--
-
The crystal structure of human phosphoserine phosphatase (HPSP) in the open conformation has been determined at a resolution of 1.53 A. The crystals are orthorhombic, belonging to space group C222(1), with unit-cell parameters a = 49.03, b = 130.25, c = 157.29 A. The asymmetric unit contains two molecules. Phase information was derived from a multiwavelength anomalous dispersion (MAD) experiment conducted at three wavelengths using a selenomethionine-derivative crystal of HPSP. The structure was refined using CNS to a final crystallographic R value of 21.6% (R(free) = 23.4%). HPSP is a dimeric enzyme responsible for the third and final step of the l-serine biosynthesis pathway. It catalyses the Mg2+-dependent hydrolysis of l-phosphoserine. Recently, the structure of HPSP in complex with an inhibitor bound to the active site has been reported to be the open conformation of the enzyme. Here, the structure of HPSP is reported in the absence of substrate in the active site. Evidence is presented that HPSP in an uncomplexed form is in an even more open conformation than in the inhibitor complex. In this state, the enzyme is partially unfolded to allow the substrate to enter the active site. Binding of the substrate causes HPSP to shift to the closed conformation by stabilizing the partially unfolded region. In the present structure a Ca2+ ion is bound to the active site and an explanation is given why HPSP is not active when in the active site Mg2+ is replaced by a Ca2+ ion.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12777757}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12777757 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12777757}}
==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Phosphoserine phosphatase]]
[[Category: Phosphoserine phosphatase]]
[[Category: Psp]]
[[Category: Psp]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:45:10 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 14:49:57 2008''

Revision as of 11:49, 27 July 2008

Image:1nnl.png

Template:STRUCTURE 1nnl

Crystal structure of Human Phosphoserine Phosphatase

Template:ABSTRACT PUBMED 12777757

About this Structure

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

Reference

High-resolution structure of human phosphoserine phosphatase in open conformation., Peeraer Y, Rabijns A, Verboven C, Collet JF, Van Schaftingen E, De Ranter C, Acta Crystallogr D Biol Crystallogr. 2003 Jun;59(Pt 6):971-7. Epub 2003, May 23. PMID:12777757

Page seeded by OCA on Sun Jul 27 14:49:57 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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